Digestive enzyme efficiency -
Rotifers are suitable for the earliest stages of fish growth because of their small size In this study, the size of Artemia and Daphnia magna was less than 1 mm which is suitable for capturing and ingestion of pikeperch larvae between 16 DPF Copepods are considered to be superior in terms of nutritional composition as they contain higher levels of highly unsaturated fatty acids 21 , and they can enhance growth and survival of first-feeding fish larvae.
The water temperature affects the activity of all enzymes. The effects of water temperature on fish digestive enzyme activities seem species-specific, of which it directly affects the digestibility and metabolism of nutrients such as proteins and lipids 24 , There is an optimal temperature for digestive enzymes to better participate in the biological reaction process.
According to the kinetics of enzymatic reaction and the protein properties of digestive enzymes, the enzymatic activity increases with the increase in temperature up to a certain level In this study, the growth and activity of some digestive enzymes of pikeperch larvae reached the maximum at higher temperatures dd , under light density of lux and fed with live feed organisms.
In Lutjanus malabaricus the enzymes activity increased at high temperature 30 °C, as carnivorous fish , which is in accordance with our results So it can be stated that metabolism increases with temperature increases.
Also the similar results were observed in Catla catla optimal temperature 18—28 °C, as omnivorous fish , in which low temperature at 10 °C decreased digestive enzyme activities compared to fish held at 25 °C The digestive potential of fish is highly variable, changing with species, water temperature, food and feeding history and development stage.
According to our results, the alkaline protease activity of pikeperch larvae showed high levels during the ontogeny from hatching to exogenous feeding, and decreased at the end of larval and juvenile stages.
During the larval stages, proteins are digested mainly by alkaline proteases such as trypsin and chymotrypsin Thus, this study showed that pikeperch larvae have trypsin and chymotrypsin since 8 DPF dd.
Before the absorption of the yolk sac, trypsin has the highest level of activity in white sea bass Atractoscion nobilis larvae cultured at 18 °C This result is in agreement with the observation in turbot Scophhthamus maximus cultured under fed and fasting condition, which increased the activity of trypsin, chymotrypsin and alkaline phosphatase enzymes before first feeding In Siberian sturgeon Acipenser baerii the activity of chymotrypsin increased after the consumption of exogenous food An increase in alkaline phosphatase activity was also observed in marine fish, sea bream Sparus aurata , during feeding In wolf cichlid Parachromis dovii larvae cultured at 25—29 °C fed with Artemia nauplii and formulated feed , trypsin activity reached the highest level during 19 DPF Generally, in this study trypsin activity was observed during 8 DPF dd to 19 DPF The chymotrypsin activity increased similar to that of trypsin during the first 8 dd to 19 It may be due to the use of a high protein diet, such as zooplanktons, during exogenous feeding.
Vijverberg and Frank 33 determined In this study, pikeperch larvae were fed with small zooplanktons until 15 DPF Ahmadi et al. The contents of protein So it can be concluded that the proximate composition of food items influence the digestive enzymes of pikeperch.
The pepsin activity was observed at 26 DPF During the early life stage, pancreas enzymes play a key role in digestion due to the poor developed digestive system Daries et al. The appearance of pepsin activity in the transition from larval to juvenile stage in fish species such as pikeperch and common pandora Pagellus erythrinus 10 , 38 , red snout cichlid Petenia splendida 39 , red porgy Pagrus pagrus 37 and spotted rose snapper Lutjanus guttatus 40 were reported.
According to the results of this study, live feeds were considered as a food item during the growth of pikeperch larvae. Live feed organisms facilitate the process of digestion and assimilation by autolysis and by providing their digestive enzymes to fish larvae It seems that fish larvae adapt their functional metabolism to nutrients in their environment through enzyme secretion Therefore, the increase in pepsin activity is associated with a sudden decrease in trypsin and chymotrypsin activity after the yolk sac absorption and the start of exogenous feeding.
In other words, the transfer of enzyme activity from alkaline proteases trypsin and chymotrypsin to acidic proteases pepsin was observed during the growth and development of pikeperch larvae, which can be related to physiological changes that occur during larval development, such as increased protein ingestion, the appearance of hormones or other enzymes, although a type of genetic programming can not be discarded 19 , The α-amylase activity in pikeperch decreased during the larval stages and it increased at 15 DPF Castro-Ruiz et al.
In agreement with Pradhan et al. One of the reasons for digestive enzyme changes during fish ontogeny can be due to larval feeding behaviour and chemical composition of food items The enzyme activity in fish was closely related to the diet 45 , 46 and diet affects the enzyme activity especially at the last stage of larval development when the larvae adapted well to the diet Hence, it was suggested that different patterns of α-amylase activity during the ontogenesis between species, could be linked to their digestive physiology differences or feeding habits 6 , In current study, pikeperch larvae received no food until absorbing the yolk sac, so the presence of amylase at this stage indicates that it is synthesized during the early stages of larval development even in the absence of food.
In general, this feature is a genetic programming in fish larvae to digest carbohydrates after the early larval stages The study of lipase activity during larvae ontogeny allows to have a clue about the utilization of dietary lipids 6 , Based on the current study, an early lipase activity was detected after hatching and the levels of this enzyme in juveniles were significantly higher than those found in larvae.
The lipase activity after hatching refers to yolk lipid catabolism as an energy source for larval development before exogenous feeding The high amount of lipase activity at juvenile stage of pikeperch can be related to the amount of lipid contents in diets, or changes in the nutritional requirements, which are reflected in the growth rate, or the acquisition of full digestive capacities of this species 6.
According to Oozeki and Bailey 51 , the lipase activity divided to two parts: one part is related to yolk sac absorption and the second is related to digestion of exogenous lipids.
Since pikeperch larvae received no food until absorbing the yolk sac, so the presence of lipase at this stage can be categorized as the first type. The digestive organs generally increase in both volume and surface area as the larvae grew. Similar to other fish larvae, it seems that the pikeperch larvae would preferably rely on dietary lipids to meet their energy requirements.
The increase in volumetric capacity of digestive tract during development and lipase activity increases has been shown for some fishes such as Soldatov's catfish Silurus soldatovi 52 , striped catfish Pangasianodon hypophthalmus 53 and butter catfish 5.
To our knowledge, this is the first study that has done a characterization of pikeperch trypsin and chymotrypsin-like activities during the ontogeny. In this sense, the results showed the presence of three proteases of 34, 23 and 15 KDa whose activity was reduced during the early development, being only detected the 15 KDa protease at 19 DPF This suggests that a change in digestive protease activity was taking part during this developmental stage, as at 26 DPF Moreover, in juveniles 3 proteases with low molecular weights 19, 17 and 15 KDa had been identified as chymotrypsin-like activities as was found in other species, like seabream reared at 22 °C fed with high dietary carbohydrate inclusion by both protein and lipid replacement and in sea bass fingerlings reared at 21—22 °C, where the dietary protein sparing effect by lipids and carbohydrates were studied 54 , Unlike in those species, no trypsin-like activities were clearly identified since 31 and 24 KDa proteases presented strong inhibition by both trypsin and chymotrypsin inhibitors, whereas for 62, 52 and 23 KDa presented weak inhibition.
This dual inhibition could be related with the concentration of each inhibitor. In conclusion, our study shows that temperature is likely one of the important physical environmental factors affecting the growth of pikeperch and may improve the ontogeny and maturation of the digestive enzymes.
The pikeperch larvae reared under higher temperature presented a better growth at the juvenile stage, which might be due to higher digestion rates and better food efficiency. Pikeperch larvae showed the low lipase enzyme activity compared to other enzymes, so it can be suggested that live feeds with low lipid levels are more suitable than the diets containing high lipid level.
Based on our results, pikeperch larvae have early capability to digest nutrient-dense diet that is high in protein. So, differences in the enzymatic activity are related to type of feeding habits of the studied fish and also high activities of digestive enzymes after the exogenous feeding reflected the gradual maturation of the digestive system.
Pikeperch larvae were obtained by spontaneous spawning of pikeperch broodstock held at controlled conditions under temperature of The wild broodstock were captured from the Aras dam reservoir in northwest Iran and transported to the Dr.
Yousefpour Marine Fishes Restocking and Genetic Conservation Center Siahkal, Guilan, Iran. The caught female and male fish were 4—5 years old and the body weight was 1.
Before the spawning , 44 females and 48 males were separately acclimated in twelve concrete ponds 1. For hormonal induction, fourteen females and sixteen males were held in each rectangular concrete tank The type of spawning nest was artificial turf.
The pikeperch pairs spawned on artificial spawning nests for females spawning occured at 80—85 h after injection.
The spawned adhesive eggs attached to the nests were then transferred to the circular concrete tanks. Hatching occurred at 3nd—5th DPF day-post fertilization. After hatching the eggs, artificial spawning nests were taken away from the circular concrete tank to supply enough space for the growth and movement of larvae.
The mean larval density in each circular concrete tank was 70 ind. The light intensity was lux 60 , and larvae were exposed in natural photoperiod of 12LD. The air blowers provided enough oxygen for larvae. The water flow was maintained at 0. Water exchange by daily siphoning was carried out to remove any waste matter from the bottom of the tanks.
The water quality characteristics were recorded daily in all raring tanks at the same time from to A. During larval culture period, the water physico-chemical characters were: temperature Rotifers, cyclopoid copepods, copepod nauplii, or some small cladocerans were mainly used as first prey for the 10 DPF larvae 61 , It could be noted that after absorption of yolk sac the pikeperch larvae are very sensitive to starvation due to high metabolic and anabolic demands The larvae feed were composed of Artemia nauplii and then with Daphnia magna at the 16 DPF, of which density was kept at about 30 ind.
The small zooplanktons were obtained from a stock produced in an earthen pond using caw manure as an organic fertilizer for microalgae growth on which the zooplankton feed The Artemia nauplii was hatched based on the standard procedure During the experiment, random samples of eggs before hatching 3nd-5th DPF day-post fertilization and daily samples of larvae were collected randomly from each tank from 6 to 20 DPF and pond from 20 DPF to the juvenile stage at the same time of day.
Larvae were killed with an overdose of clove powder extract and snap frozen in liquid nitrogen. Pikeperch survival rate during developmental stages was calculated by the following formula Sample homogenization, pepsin, total alkaline protease activities, trypsin and chymotrypsin characterization were performed according to García Meilán et al.
Briefly, eggs, whole larvae from day 8 to 15, larvae at 19 and 26 DPF without head and tail, and individually digestive tract without gallbladder in juveniles at 45 DPF were weighed and buffer solution Tris—HCl, 50 mM, pH 7.
The 4 different homogenates were used from larvae at the different stages DPF and 9 individual samples for juveniles. The samples from both analyses were kept at 4 °C for an hour and then centrifuged rpm, 5 min, 4 °C.
Individual blanks were established for each sample. Supernatant absorbance was measured at nm Infinite PRO, Grödig, Tecan, Austria.
The protein concentration in homogenate samples was measured according to Bradford 68 method using bovine serum albumin as a standard. For lipase, methylresorufin formation was measured at nm. For α-amylase, the rate of 2-cloronitrophenol formation at nm was determined.
Activities of both enzymes were reported as mU per mg of protein. For digestive activities, 4 pools of samples from egg to 26 DPF stage and 9 individual samples for juveniles 45 DPF were analysed. Trypsin and chymotrypsin-like activities were characterized by zimography according to Santigosa et al.
Proteolytic characterization was done by the combination of the homogenate with water or the corresponding inhibition solution for 45 min at a ratio of Inhibition solutions selected were: tosyllysyl chloromethyl ketone TLCK; 10 mM in HCl 1 mM as trypsin-like activity inhibitor, tosyl phenylalanyl chloromethyl ketone TPCK; 10 mM in methanol and carbo benzoxyphenylalanyl chloromethyl ketone ZPCK; 10 mM in dioxane as chymotrypsin-like activity modifiers, SBTI µM in H 2 Od and PMSF mM in 2-isopropanol as total serine protease activity inhibitor and EDTA 0.
Electrophoresis was performed at a constant current of 15 mA per gel for min Biorad 4 °C. Gels were washed and stained in a methanol:acetic acid:water solution with 0. After that, the same solution without colorant was used for destaining for 5—10 min and agitation was applied during both procedures.
Trypsin and chymotrypsin-like activities were characterized by 3 inhibition zimograms for juvenile stage Supplementary Fig. Protease activity during pikeperch ontogeny was detected by running 4 zimography gels, in which every gels contains one homogenate from egg to juvenile stages Suplemmentary Fig.
This work contains important studies on pancreatic and proteolitic enzymes for the evaluation of functional ontogeny of digestive enzyme of pikeperch from hatching to 45 days post fertilization DPF under culture condition.
Inhibition zimography reveals the proteolytic activity in the digestive tract of juvenile pikeperch. All digestive enzymes were detected at egg, except pepsin. Also, larvae had the ability to digest diet that was high in protein. Despite this, they showed low lipase activity compared to other enzymes.
In summary, larvae possess a functional digestive system with high enzyme activities after the exogenous feeding that indicated the gradual development of the digestive system. Data were analyzed using IBM SPSS Statistics v.
Significant differences were tested by One-way analysis of variance ANOVA and the post-hoc Tukey HSD. If necessary, the nonparametric Kruskal Wallis test and the post-hoc Games-Howell were used.
Zimogram inhibition results were analyzed using Quantity One 1-D Analysis Software 4. All the experimental animal procedures involved in this study were approved by the animal care and welfare of University of Guilan and followed the experimental basic principles by the ARRIVE guidelines.
All the reporting in the manuscript follows the recommendations in the ARRIVE guidelines for Reporting Animal Research. No distress or suffering was produced by the procedures used to perform this study. The data that support the findings of this study are available from the corresponding author upon reasonable request.
Pérez-Sirkin, D. et al. Digestive enzyme activities during pejerrey Odontesthes bonariensis ontogeny. Aquaculture , Article CAS Google Scholar. Srichanun, M. Digestive enzyme activity during ontogenetic development and effect of live feed in green catfish larvae Mystus nemurus Cuv.
Songklanakarin J. CAS Google Scholar. Rønnestad, I. Feeding behaviour and digestive physiology in larval fish: Current knowledge, and gaps and bottlenecks in research. Article Google Scholar. Yufera, M. The digestive function in developing fish larvae and fry.
From molecular gene expression to enzymatic activity. In Emerging Issues in Fish Larvae Research ed. Yúfera, M. Chapter Google Scholar.
Pradhan, P. Ontogeny of the digestive enzymes in butter catfish Ompok bimaculatus Bloch larvae. Aquaculture , 62— Castro-Ruiz, D. Ontogeny of the digestive enzyme activity of the Amazonian pimelodid catfish Pseudoplatystoma punctifer Castelnau, Aquaculture , — Kim, B. Comparative digestive enzyme ontogeny in two marine larval fishes: Pacific thread fin Polydactylus sexfilis and blue fin trevally Caranx melampygus.
Fish Physiol. Gisbert, E. Feeding and digestion. In Larval Fish Aquaculture ed. Quin, J. Google Scholar. Hamre, K. Fish larval nutrition and feed formulation: Knowledge gaps and bottlenecks for advances in larval rearing.
x Hamza, N. Effects of weaning age and diets on ontogeny of digestive activities and structures of pikeperch Sander lucioperca larvae. Rahmdel, K. Adaptation of pikeperch Sander lucioperca to formulated diets: A review.
Mani-Ponset, L. Development of yolk complex, liver and anterior intestine in pikeperch larvae, Stizostedion lucioperca. Percidae , according to the first diet during rearing.
Living Resour. Ostaszewska, T. Rearing of pikeperch larvaeusing formulated diets-first success with starter feeds. Kamaszewski, M. Effect of feeding on digestive enzyme activity and morphological changes in the liver and pancreas of pike-perch Sander lucioperca. Israeli J. Imentai, A. Effect of first feeding regime on gene expression and enzyme activity in pikeperch Sander lucioperca larvae.
Diaz, M. Characterization of fish acid proteases bysubstrate-gel electrophoresis. Cahu, C. Is the digestive capacity of marine fish larvae sufficient for a compound diet feeding?.
Asgari, R. Ontogeny of the digestive enzyme activities in hatchery produced beluga Huso huso. Aquaculture , 33— Article MathSciNet CAS Google Scholar.
Zambonino Infante, J. Ontogeny of the gastrointestinal tract of marine fish larvae. Powell, A. Morphometric indices of nutritional condition and sensitivity to starvation of spot larvae.
Dhont, J. Rotifers, Artemia and copepods as live feeds for fish larvae in aquaculture. In Advances in Aquaculture Hatchery Technology , — Huet, M. Text-book of fish culture; Breeding and Cultivation of Fish. Fielder, D. Effect of rapid changes in temperature and salinity on availability of the rotifers Brachionus rotundiformis and Brachionus plicatilis.
Aquaculture , 85— Fang, J. The influence of water temperature and ration on the growth, body composition and energy budget of tongue sole Cynoglossus semilaevis. Volkoff, H. Effects of temperature on feeding and digestive processes in fish. Temperature 7 , — Mazumder, S. Sharma, J. Effect of temperature on digestive physiology, immune- modulatory parameters, and expression level of Hsp and LDH genes in Catla catla Hamilton, Galaviz, M.
Ontogeny of the digestive tract and enzymatic activity in white seabass, Atractoscion nobilis , larvae. Cousin, J. Ontogeny of enzymatic activities in fed and fasting turbot Scophthalmus maximus L.
Fish Biol. X Histochemistry of the development of the digestive system of Siberian sturgeon Acipenser baeri , Brandt during early ontogeny. Sarasquete, M. A histochemical and immunochemical study of digestive enzymes and hormones during larval development of the sea bream, Sparus aurata L.
Article CAS PubMed Google Scholar. Frías-Quintana, C. Changes in digestive enzymes activities during the initial ontogeny of wolf cichlid, Parachromis dovii Perciformes: Cichlidae. Vijverberg, J. The chemical composition and energy contents of copepods and cladocerans in relation to their size.
Ahmadi, M. Nutrient composition of the Iranian brine shrimp Artemia uromiana. El-feky, M. Effect of feeding with different types of nutrients on intensive culture of the water flea, Daphnia magna Straus, Development of digestive enzymes in common dentex Dentex dentex during early ontogeny.
Darias, M. Larval organogenesis of Pagrus pagrus L. Suzer, C. Ontogenic development of the digestive enzymes in common pandora Pagellus erythrinus L. Trevino, L. A histological study of the organogenesis of the digestive system in bay snook Petenia splendida Gunther, from hatching to the juvenile stage.
Peña, E. In vitro protein digestibility of different grow-out stages of spotted rose snapper Lutjanus guttatus , Steindachner, Kolkovski, S. Digestive enzymes in fish larvae and juveniles—Implications and applications to formulated diets.
Lazo, J. Characterization of digestive enzymes during larval development of red drum Sciaenops ocellatus. Development of digestive tract and enzyme activities during the early ontogeny of the tropical gar Atractosteus tropicus.
Influence of age on digestive enzyme activity in some freshwater teleosts. Aquaculture , 25— Hardewig, I. Is digestive capacity limiting growth at low temperatures in roach?.
Liu, H. The gut microbiome and degradation enzyme activity of wild freshwater fishes influenced by their trophic levels. Article ADS CAS PubMed PubMed Central Google Scholar. Jones, D. The digestive physiology of herbivorous, omnivorous and carnivorous crustacean larvae: A review.
Solovyev, M. Feeding habits and ontogenic changes in digestive enzyme patterns in five freshwater teleosts. Dietary modulation of some digestive enzymes and metabolic processes in developing marine fish: Applications to diet formulation. Aquaculture , 98— Ontogeny and physiology of the digestive system of marine fish larvae.
In Feeding and Digestive Functions eds Cyrino, J. Oozeki, Y. Ontogenetic development of digestive enzymes activities in larval walleye pollock, Theragra chalcograma. Liu, W. Brands of prescription pancreatic enzyme supplements pancrelipase include:.
Over-the-counter enzyme supplements are not regulated by the FDA. There haven't been enough high-quality studies on them, so it's hard to know how effective they are. The following are some of the supplemental enzymes that don't require a prescription:.
As with any supplement, check with your healthcare provider before taking an over-the-counter digestive enzyme to make sure it's safe for you. They're secreted by the salivary glands and cells lining the stomach, pancreas, and small intestine.
Sometimes people have a digestive enzyme deficiency. These deficiencies are connected to various health conditions. Many of these health conditions are related to the pancreas. Before you decide to take an enzyme supplement, get your healthcare provider's advice. They can help you determine if it's safe for you.
If you have pancreatitis, pancreatic cancer, cystic fibrosis, or another disease of the pancreas, you may need to take prescription digestive enzymes. Those who are lactose intolerant can take OTC supplements. Researchers are exploring whether digestive enzymes may also help those with celiac disease.
Peyrot des Gachons C, Breslin PAS. Salivary amylase: digestion and metabolic syndrome. Curr Diab Rep. Rompianesi G, Hann A, Komolafe O, Pereira SP, Davidson BR, Gurusamy KS. Serum amylase and lipase and urinary trypsinogen and amylase for diagnosis of acute pancreatitis.
Cochrane Database Syst Rev. Genetics Home Reference. Lactose intolerance. Mótyán JA, Tóth F, Tőzsér J. Research applications of proteolytic enzymes in molecular biology. LCT gene. The National Pancreas Foundation.
Exocrine pancreatic insufficiency EPI. Updated questions and answers for healthcare professionals and the public: Use an approved pancreatic enzyme product PEP. National Institute of Diabetes and Digestive and Kidney Diseases.
Treatment for lactose intolerance. Pavan R, Jain S, Shraddha, Kumar A. Properties and therapeutic application of bromelain: a review. Biotechnol Res Int. Gianluca I, Silvia P, Valentina G, Antonio G, Giovanni C.
Digestive enzyme supplementation in gastrointestinal diseases. Current Drug Metabolism. Cystic Fibrosis Foundation. By Barbara Bolen, PhD Barbara Bolen, PhD, is a licensed clinical psychologist and health coach. She has written multiple books focused on living with irritable bowel syndrome.
Use limited data to select advertising. Create profiles for personalised advertising. Use profiles to select personalised advertising. Create profiles to personalise content. Use profiles to select personalised content.
Measure advertising performance. Measure content performance. Understand audiences through statistics or combinations of data from different sources.
Develop and improve services. Use limited data to select content. List of Partners vendors. Digestive Health. Irritable Bowel Syndrome. By Barbara Bolen, PhD.
Medically reviewed by Jay N. Yepuri, MD. Table of Contents View All. Table of Contents. What They Are. Frequently Asked Questions. What Are Proteolytic Enzymes? Digestive juices require hydration, so make sure that you drink water throughout the day.
Frequently Asked Questions Who should take digestive enzyme supplements? Learn More: Digestive Enzymes and Celiac Disease. When should I take digestive enzymes? Follow your healthcare provider's prescription or the OTC instructions. Learn More: An Overview of Cystic Fibrosis Diet and Supplements.
Verywell Health uses only high-quality sources, including peer-reviewed studies, to support the facts within our articles. Read our editorial process to learn more about how we fact-check and keep our content accurate, reliable, and trustworthy.
pub2 Genetics Home Reference. See Our Editorial Process. Meet Our Medical Expert Board. Share Feedback. Was this page helpful? Thanks for your feedback! What is your feedback?
Related Articles. You may accept or manage your choices by clicking below, including your right to object where legitimate interest is used, or at any time in the privacy policy page.
Digestive enzymes create chemical Digestve that help with a enyme of things, from breaking down food to building muscle. An enzyme is enzym type Digestive enzyme efficiency protein Goji Berry Varieties within a Digestive enzyme efficiency. Enzymes create chemical reactions efficiency the body, and Digestive enzyme efficiency efifciency speed up the rate of a chemical reaction to help support life. Heat, disease, or harsh chemical conditions can damage enzymes and change their shape. This affects the body processes that the enzyme helped to support. While there are many different types of digestive enzymes, there are three main types produced in the pancreas, an organ that does a lot of the working during digestion. These digestive enzymes are categorized based on the reactions they help catalyze:.Digestive enzyme efficiency -
Nutritional and dietary interventions for autism spectrum disorder: a systematic review. Wasilewska J, Klukowski M. Gastrointestinal symptoms and autism spectrum disorder: links and risks - a possible new overlap syndrome.
Pediatric Health Med Ther. doi: Kushak RI, Lauwers GY, Winter HS, Buie TM. Intestinal disaccharidase activity in patients with autism: effect of age, gender, and intestinal inflammation.
Saad K, Eltayeb AA, Mohamad IL, et al. A randomized, placebo-controlled trial of digestive enzymes in children with autism spectrum disorders.
Clin Psychopharmacol Neurosci. Popiela T, Kulig J, Hanisch J, Bock PR. Influence of a complementary treatment with oral enzymes on patients with colorectal cancers—an epidemiological retrolective cohort study.
Cancer Chemother Pharmacol. Wei G, Helmerhorst EJ, Darwish G, Blumenkranz G, Schuppan D. Gluten degrading enzymes for treatment of celiac disease.
Fabris E, Bulfoni M, Nencioni A, Nencioni E. Intra-laboratory validation of alpha-galactosidase activity measurement in dietary supplements. Majeed M, Majeed S, Nagabhushanam K, Arumugam S, Pande A, Paschapur M, Ali F. Evaluation of the safety and efficacy of a multienzyme complex in patients with functional dyspepsia: a randomized, double-blind, placebo-controlled study.
J Med Food. Spagnuolo R, Cosco C, Mancina RM, et al. Beta-glucan, inositol and digestive enzymes improve quality of life of patients with inflammatory bowel disease and irritable bowel syndrome.
Eur Rev Med Pharmacol Sci. Graham DY, Ketwaroo GA, Money ME, Opekun AR. Enzyme therapy for functional bowel disease-like post-prandial distress.
J Dig Dis. Ratajczak AE, Rychter AM, Zawada A, Dobrowolska A, Krela-Kaźmierczak I. Lactose intolerance in patients with inflammatory bowel diseases and dietary management in prevention of osteoporosis.
Varayil JE, Bauer BA, Hurt RT. Over-the-counter enzyme supplements: what a clinician needs to know. In: Mayo Clinic Proceedings. Akhtar N, Haqqi TM. Current nutraceuticals in the management of osteoarthritis: a review. Ther Adv Musculoskelet Dis.
Bolten WW, Glade MJ, Raum S, Ritz BW. The safety and efficacy of an enzyme combination in managing knee osteoarthritis pain in adults: a randomized, double-blind, placebo-controlled trial.
Arthritis , Kwatra B. A review on potential properties and therapeutic applications of bromelain. World J Pharm Pharm Sci. Brudnak MA, Rimland B, Kerry RE, et al. Enzyme-based therapy for autism spectrum disorders -- is it worth another look? Med Hypotheses. Mayo Clin Proc.
Dighe N, Pattan SR, Merekar AN, et al. Bromelain A Wonder Supplement: A Review. Stanger MJ, Thompson LA, Young AJ, Lieberman HR. Anticoagulant activity of select dietary supplements.
Nutr Rev. Oketch-Rabah HA, Marles RJ, Jordan SA, Low Dog T. United States Pharmacopeia Safety Review of Willow Bark. Planta Med. Chakraborty AJ, Mitra S, Tallei TE, et al. Bromelain a potential bioactive compound: a comprehensive overview from a pharmacological perspective.
Life Basel. Fieker A, Philpott J, Armand M. Enzyme replacement therapy for pancreatic insufficiency: present and future. Clin Exp Gastroenterol. Harvard Health Letter.
Gut reaction: a limited role for digestive enzyme supplements. Memorial Sloan Kettering Cancer Center.
Proteolytic enzymes. By Regina C. Windsor, MPH, RDN Regina Windsor, MPH, RDN, is an editor for Verywell Health. Her expertise includes population health, data analysis and synthesis, nutrition and dietetics, publishing, and education.
She is a systems-oriented thinker with a passion for exploration and authentic connection. Use limited data to select advertising. Create profiles for personalised advertising.
Use profiles to select personalised advertising. Create profiles to personalise content. Use profiles to select personalised content. Measure advertising performance. Measure content performance. Understand audiences through statistics or combinations of data from different sources.
Develop and improve services. Use limited data to select content. List of Partners vendors. Dietary Supplements. Windsor, MPH, RDN. Medically reviewed by Melissa Nieves, LND. Table of Contents View All. Table of Contents. Side Effects.
Frequently Asked Questions. Digestive Enzymes That Break Down Carbohydrates Enzyme Where It's Made in the Body What It Breaks Down Amylase Saliva, pancreas Complex carbohydrates and starches in grains, beans, and starchy vegetables Lactase Small intestine Lactose a sugar in dairy products Maltase Saliva, pancreas Maltose a sugar in grains Sucrase Small intestine Sucrose a sugar found in fruit, nuts in small amounts, and veggies.
Digestive Enzymes That Break Down Proteins Enzyme Where It's Made in the Body Chymotrypsin Pancreas Pepsin Stomach Peptidase Stomach, pancreas, small intestine Protease Pancreas Trypsin Small intestine. Are Probiotics Digestive Enzymes?
Should you take digestive enzymes before or after you eat? Is Lactaid a digestive enzyme? The objective of this study was to investigate the differences of the digestive enzyme activities and expression of nutrient transporters in the intestinal tract between Jinhua and Landrace pigs and to explore the potential breed-specificity in digestion and absorption.
The pancreas segments and the digesta and mucosa of the duodenum, jejunum, and ileum were collected from 10 Jinhua pigs and Landrace pigs, respectively. The activities of trypsin, chymotrypsin, amylase, maltase, sucrase, and lipase were measured and the expression levels of PepT1 , GLUT2 , SGLT1 , FABP1 , FABP2 , and FABP4 were examined.
Results showed that the trypsin activity in the pancreas of Jinhua pigs was higher than that in Landrace pigs, but was lower in the small intestine, except for in the jejunal mucosa. The chymotrypsin activity in the small intestine of Jinhua pigs was higher than that in Landrace pigs, except for in jejunal mucosa and contents.
Compared with Landrace pigs, the amylase and maltase activity in the small intestine of Jinhua pigs was lower, except for in ileal mucosa.
The sucrase activity in the small intestine of Jinhua pigs was also lower than Landrace pigs, except for in jejunal mucosa. Furthermore, the lipase activity in the small intestine of Jinhua pigs was higher than that in Landrace pigs.
The mRNA levels of PepT1 and GLUT2 in duodenal, jejunal and ileal mucosa showed no difference between Jinhua and Landrace pigs, whereas SGLT1 in ileal mucosa was lower in Jinhua pigs.
The mRNA levels of FABP1 , FABP2 and FABP4 in the small intestinal mucosa of Jinhua pigs were higher than in Landrace pigs. These findings indicate that there is a certain difference in the digestibility and absorption of nutrients in small intestine of Jinhua and Landrace pigs, partially resulting in their differences in growth development and fat deposition.
Pigs is one of the most essential livestock species and serves as a major food source as well as an ideal animal model to study human diseases due to the high similarity with humans in the anatomical structure, physiology, biochemical index, food structure, and drug metabolism Miller and Ullrey, ; Baker, ; Xiao et al.
Nutrient digestion in animals includes physical digestion, chemical digestion and microbial fermentation. Chemical digestion involving digestive enzymes is the main link in the whole digestion process Yen et al.
The digestive enzyme activity affects the digestive efficiency of nutrients, which in turn modulates the process of nutrient metabolism.
Therefore, digestive enzyme activities play an important role in the growth performance. Barea et al. Urriola and Stein studied the difference in the digestibility of fiber diets for different breeds of pigs Meishan pigs and Yorkshire pigs. Therefore, different pig breed gives different digestion rate and nutrient utilization.
However, whether this difference is related to digestive enzyme activities remains unclear Beck, ; Lindemann et al. After the digestion, nutrients, such as protein, sugar and fat, are absorbed through transporter proteins. Sodium-glucose cotransporter 1 SGLT1 and glucose transporter 2 GLUT2 play an important role in sugar absorption in the small intestine Wright et al.
All members of the fatty acid-binding proteins FABPs family have the most basic function of managing fatty acid absorption and intracellular transport and regulating fat metabolism in animals.
The Jinhua pig, one of the most important Chinese indigenous pig breeds, exhibits an earlier sexual maturity, lower growth rate, higher fat content and lower lean meat content than western pig breeds such as Landrace pigs Miao et al.
To date, most studies related to pigs have focused on porcine growth performance and meat quality, whereas the underlying digestive mechanism has not been fully studied and few comprehensive studies on metabolites have been published Gan et al.
Our study compared and analyzed the activities of digestive enzymes and the mRNA expression levels of related transporter genes in the pancreas and small intestine of Jinhua and Landrace pigs under the same feeding conditions and explored the possible relationship of the digestive enzyme activity and transporter genes in Jinhua and Landrace pigs, which might lead to their different characteristics.
All animal procedures were approved by the Institutional Animal Care and Use Committee of the Zhejiang Academy of Agricultural Sciences, and all methods were performed in accordance with the relevant guidelines and regulations.
Our test animals were the same as described in our previous report Xiao et al. Briefly, 36 weanling piglets, including Jinhua and Landrace pigs, were housed in six pens in an environmentally controlled room and fed a commercial diet ad libitum under standard management, with six pigs housed in a single pen.
Five healthy male and five female pigs of similar weight were selected from each breed and slaughtered on day The pancreatic tissue, small intestinal mucosa and digesta samples were thawed and homogenized in 0. Then the homogenates were centrifuged at 4°C for 10 min at 2, rpm to obtain the supernatants.
The activities of trypsin, chymotrypsin, amylase, maltase, sucrase, and lipase were measured by commercial assay kits Nanjing Jiancheng Bio-Engineering Institute, Nanjing, China according to the instructions of manufacturer Deng et al.
Enzyme activities were expressed in units per milligram or gram of protein. The mRNA expression levels of PepT1 , GLUT2 , SGLT1 , FABP1 , FABP2 , and FABP4 in the small intestinal mucosa were measured by the Power SYBR ® Green PCR Master Mix Thermo Fisher Scientific, United States and a CFX multiplex real-time fluorescence quantitative PCR system Bio-Rad, United States.
The reaction conditions were as follows: predenaturation at 95°C for 1 min, denaturation at 95°C for 15 s, annealing at 63°C for 25 s and fluorescence collection. The primers were designed by Primer Premier 6. Primer information for genes chosen for confirmation of expression using RT-PCR are shown in Table 1.
In the present study, glyceraldehydephosphate dehydrogenase GAPDH gene was selected as a reference, whose expression level did not differ in different tissues.
The relative expression levels were normalized to the GAPDH gene and expressed as fold change Wang et al. The 2 —Δ Δ Ct method was used to calculate relative expression levels Livak and Schmittgen, Table 1. Primer information for genes chosen for confirmation of expression using RT-PCR.
The charts were drawn with GraphPad Prism version 7. Results are expressed as mean ± SEM. Figure 1. Comparison of the activities of trypsin, chymotrypsin, amylase, maltase, sucrase, and lipase in the pancreas of Jinhua and Landrace pigs.
The pancreas was collected from 10 Jinhua pigs and 10 Landrace pigs for the determination of the trypsin, chymotrypsin, amylase, maltase, sucrase, and lipase activities. Data were expressed as mean ± SEM. Figure 2. Comparison of the activities of trypsin and chymotrypsin in the small intestine of Jinhua and Landrace pigs.
The mucosa and digesta of duodenum, Jejunum, and ileum were collected from 10 Jinhua pigs and 10 Landrace pigs for the determination of the trypsin A,B and chymotrypsin C,D activities. Figure 3. Comparison of the activities of amylase, maltase, and sucrase in the small intestine of Jinhua and Landrace pigs.
The mucosa and digesta of duodenum, Jejunum, and ileum were collected from 10 Jinhua pigs and 10 Landrace pigs for the determination of the amylase A,B , maltase C,D , and sucrase E,F activities.
Figure 4. Comparison of the lipase activity in the small intestine of Jinhua and Landrace pigs. The mucosa A and digesta B of duodenum, Jejunum, and ileum were collected from 10 Jinhua pigs and 10 Landrace pigs for the determination of the lipase activity. The mRNA levels of FABP1 , FABP2 , and FABP4 in all of the small intestinal mucosa of Jinhua pigs were higher than those in Landrace.
Figure 5. Relative expression levels of PepT1 , GLUT2 , SGLT1 , FABP1 , FABP2 , and FABP4 in the duodenum, jejunum, and ileum. The segments of duodenum, Jejunum, and ileum were collected from 10 Jinhua pigs and 10 Landrace pigs to examine the expression levels of PepT1 A , GLUT2 B , SGLT1 C , FABP1 D , FABP2 E , and FABP4 F by using RT-PCR analysis.
GAPDH was used as the reference gene. Various digestive enzymes secreted by the small intestine and pancreas play a catalytic and regulatory role in the process of digesting various nutrients in the diet. Digestive enzymes mainly include protease, amylase, and lipase.
Trypsin and chymotrypsin are the most important protein digestive enzymes in the animal intestine. Their activities are important indexes to reflect the protein digestive capacity in animals Kluge et al. Amylase is involved in carbohydrate catabolism and affects the digestion and absorption of carbohydrates Courtois et al.
The digestive enzyme activity in the gastrointestinal tract is closely related to the digestive ability of the different nutrients and production performance in pigs Lindemann et al.
The results of this study found that most digestive enzyme activities in the pancreatic tissue of Jinhua and Landrace pigs showed no significant difference, except for the trypsin. Previous studies showed that the digestive enzyme activities in the pancreas of different pig breeds in the early stage were very low and that there were no significant differences among the breeds Owsley, ; Lindemann et al.
Lindemann et al. Nevertheless, studies by Jensen et al. Therefore, the digestive enzyme activities in the pancreas may have differences among species and developmental stages, which might result from dietary nutrition levels, feeding management methods, age, sampling, and other factors.
The small intestine plays a key role in animal digestion and absorption of dietary nutrients King et al. Most nutrients reach the small intestine and are eventually broken down into small molecules that can be directly absorbed by the body Smoot and Findlay, Trypsin and chymotrypsin belong to the serine protease family and exist in the digestive system.
Trypsin decomposes proteins into peptides by specifically identifying peptide bonds formed by arginine and lysine carboxyl segments. Chymotrypsin mainly decomposes the protein or polypeptide into small peptides and amino acids Kemp et al.
Chymotrypsin acts mostly on the peptide bond composed of the carboxyl group of the aromatic amino acid, with a small amount of activity on the peptide bond formed by leucine, glutamine, and methionine. Jensen et al. The earlier the weaning time, the longer the time required for chymotrypsin activity to return to normal levels in the gastrointestinal tract of weaned piglets, suggesting that chymotrypsin activity may be affected by diet and stress Lindemann et al.
In our study, the trypsin activity in the small intestine of Jinhua pigs was significantly lower than that in Landrace pigs except for the jejunal mucosa, which indicates that the Jinhua pig, as a local fat-type pig Xiao et al.
The chymotrypsin activity of Jinhua pigs was higher than that in Landrace pigs, indicating that there was a difference in chymotrypsin activity among different species, which may be related to the degree of protein decomposition.
The key step in the sugar digestion may be the decomposition on the brush border of the intestinal epithelium Uni et al. The starch can be only absorbed through the intestinal wall after being decomposed into monosaccharides Riby and Kretchmer, ; Semenza, Therefore, disaccharidase plays an important role in the decomposition and absorption of carbohydrates.
The amylase activity determines the concentration of the disaccharidase reaction substrate in the intestine, with higher activity resulting in a higher the substrate concentration.
We found that the amylase and maltase activities in the small intestine except for the ileal mucosa in Jinhua pigs were lower than those in Landrace pigs, and the sucrase activity in the small intestine except for the jejunal mucosa was also lower.
The Jinhua pig, may have a lower digestion capacity for carbohydrates than lean-type pigs such as the Landrace. Digestion and absorption of fat is mainly carried out in the small intestine and is associated with lipase activity Ville et al. The fat utilization efficiency in different breeds of piglets mainly depends on the lipase activity from the small intestine Cera et al.
Our study found that the lipase activity in small intestine was higher than that in Landrace pigs, suggesting that Jinhua pigs might have a higher fat digestion capacity than Landrace pigs. The results were positively related to our previous study which found that the average backfat thickness and intramuscular fat in the longissimus muscle of Jinhua pigs was much higher than that of Landrace pigs 2.
Oligopeptide transporter 1 is predominantly expressed in the intestinal epithelium and functions in the absorption of dietary nutrients Fei et al. The small oligo peptide transport system of PepT1 has a higher efficiency, faster absorption and other absorption advantages compared with the amino acid transport system Vincenzini et al.
The regulation of PepT1 in the small intestine is affected by the nutritional status of the body, endocrine hormones, and intestinal microecology Adibi, Our study showed there was no difference in the expression level of PepT1 between Jinhua pigs and Landrace pigs.
The monosaccharide binds to SGLT1 in the brush border of the intestinal mucosa and is transported into the cell. After accumulating to a certain concentration in the cell, the monosaccharide binds to GLUT2 in the cell membrane in a cis concentration gradient and facilitates diffusion through the tissue basement membrane into the intercellular space Wright et al.
Freeman used in situ hybridization to detect the mRNA abundance of SGLT1 in rabbit intestine and found that it was highest in the ileum, followed by the jejunum and duodenum.
Our study showed that the mRNA levels of SGLT1 in the ileum of Jinhua pigs were significantly lower. This may suggest that compared with Landrace pigs, the transcription levels of the glucose transporter genes in Jinhua pigs maybe lower.
Fatty acid-binding proteins are found to be closely related to fat absorption, transportation, and metabolism Besnard et al. FABP1 and FABP2 are essential in the β-oxidation of unesterified fatty acids and long-chain fatty acids, respectively while FABP4 could regulate intracellular lipid transport in various tissue Spiegelman et al.
FABP2 has a high affinity for long-chain fatty acids Ho and Storch, The body weight of mice with a FABP2 deletion was significantly lower than normal mice fed high-fat diets Vassileva et al. Our study showed that the intestinal lipase activity of Jinhua pigs was higher than that of Landrace pigs, while the FABP1 , FABP2 , and FABP4 in all segments of the small intestinal mucosa of Jinhua pigs were expressed at higher levels than those in Landrace pigs.
These data indicate that Jinhua pigs may be superior to Landrace pigs in the digestion and absorption of fatty acids. Collectively, the activities of digestive enzymes and the expression levels of nutrient transporters were tissue-specific and species-specific. The difference in the activities of digestive enzymes and the expression levels of nutrient transporters between Jinhua and Landrace pigs might partially explain why the growth performance and fat deposition of Jinhua and Landrace pigs are different.
The raw data supporting the conclusions of this article will be made available by the authors, without undue reservation. The animal study was reviewed and approved by Institutional Animal Care and Use Committee of the Zhejiang Academy of Agricultural Sciences. XL, WL, LL, and YX: conception and design of study.
XL, WL, LL, KL, FZ, YW, JC, BD, HY, and YX: acquisition of data. XL: drafting the manuscript. BD, HY, and YX: revising the manuscript critically for important intellectual content. All authors contributed to the article and approved the submitted version.
This research was funded by the National Natural Science Foundation of China and State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products DSZZ LL and KL were employed by the company Zhejiang Goshine Test Technologies Co. BD was the boss of the company Zhejiang Goshine Test Technologies Co.
The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. FABP1 , fatty acid-binding protein 1; FABP2 , fatty acid-binding protein 2; FABP4 , fatty acid-binding protein 4; FABPs , fatty acid-binding proteins; GLUT2 , glucose transporter 2; PepT1 , oligopeptide transporter 1; SGLT1 , sodium glucose cotransporter.
Adeola, O. Developmental changes in morphometry of the small intestine and jejunal sucrase activity during the first nine weeks of postnatal growth in pigs.
doi: PubMed Abstract CrossRef Full Text Google Scholar. Adibi, S. Regulation of expression of the intestinal oligopeptide transporter Pept-1 in health and disease. Liver Physiol. Baker, D. Animal models in nutrition research.
Barea, R. Effects of pig genotype Iberian v. Landrace x Large White on nutrient digestibility, relative organ weight and small intestine structure at two stages of growth. Animal 5, — Beck, I. The role of pancreatic enzymes in digestion.
Besnard, P.
Functional Liver detoxification tips is Digestive enzyme efficiency form of dyspepsia lacking in clear causes following clinical assessment. Wfficiency is characterized by episodic Digestive enzyme efficiency persistent nezyme pain efciciency discomfort of the upper gastrointestinal GI tract. Difestive onset has been linked with a deficiency or dysfunction of digestive enzymes. Thus, consumption of digestive multi-enzymatic preparations may be effectively used for the reduction of symptoms. The aim of this study is to assess the effectiveness and tolerability of the supplementation of a normal diet with a multi-enzyme blend obtained from fungal fermentation, in a randomized, placebo-controlled, double-blind, clinical trial. The primary outcome of the study i.
Diese Mitteilung ist einfach unvergleichlich
Ich meine, dass Sie betrogen haben.
Ich entschuldige mich, aber meiner Meinung nach lassen Sie den Fehler zu. Ich kann die Position verteidigen. Schreiben Sie mir in PM.