Results 11 to 20 of about 119,725 (278)

Evaluation of the inhibitory potential of pro-peptide region as the inhibitor of the digestive chymotrypsin of cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae), based on in silico studies [PDF]

open access: yesنامه انجمن حشره‌شناسی ایران, 2020
The cotton bollworm, Helicoverpa armigera (Hübner),is a wide host range pest that causes severe economic damages to agricultural crops in Iran and all around the world.
S. A. Hemmati, N. Karam Kiani
doaj   +1 more source

Safety evaluation of a food enzyme containing trypsin and chymotrypsin from porcine pancreas

open access: yesEFSA Journal, 2021
The food enzyme is a serine protease complex containing trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1) obtained from porcine pancreas by Paninkret Chem.‐Pharm. Werk GmbH.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +27 more
doaj   +2 more sources

Characterization and expression analysis of chymotrypsin after bacterial challenge in the mud crab, Scylla paramamosain [PDF]

open access: yesGenetics and Molecular Biology, 2014
Chymotrypsin is one of the serine proteases families that have various biological functions. A chymotrypsin gene was isolated from hepatopancreas of the mud crab, Scylla paramamosain (designated SpCHY) in this study.
Jie Gong   +5 more
doaj   +3 more sources

Detection of Chymotrypsin by Optical and Acoustic Methods

open access: yesBiosensors, 2021
Chymotrypsin is an important proteolytic enzyme in the human digestive system that cleaves milk proteins through the hydrolysis reaction, making it an interesting subject to study the activity of milk proteases.
Ivan Piovarci   +2 more
doaj   +1 more source

Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme

open access: yesTropical Animal Science Journal, 2021
The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE).
T. R. Hakim   +7 more
doaj   +1 more source

Loss of chymotrypsin-like protease (CTRL) alters intrapancreatic protease activation but not pancreatitis severity in mice

open access: yesScientific Reports, 2020
The digestive enzyme chymotrypsin protects the pancreas against pancreatitis by reducing harmful trypsin activity. Genetic deficiency in chymotrypsin increases pancreatitis risk in humans and pancreatitis severity in mice.
D. Mosztbacher   +2 more
semanticscholar   +1 more source

Casein Proteolysis in Bioactive Peptide Production: Optimal Operating Parameters [PDF]

open access: yesТехника и технология пищевых производств, 2020
Introduction. Public health is gradually deteriorating as a result of unhealthy lifestyle and diet, which triggers allergic reaction to certain foods.
Milentyeva Irina S.   +2 more
doaj   +1 more source

Biological Evaluation and Conformational Preferences of Ferrocene Dipeptides with Hydrophobic Amino Acids

open access: yesInorganics, 2023
Despite the large number of peptidomimetics with incorporated heteroannularly functionalized ferrocenes, few studies have investigated their bioactivity.
Monika Kovačević   +10 more
doaj   +1 more source

Identification and characterisation of gut proteases in the fig tree skeletoniser moth, Choreutis nemorana Hübner (Lepidoptera: Choreutidae)

open access: yesPlant Protection Science, 2013
The biochemical properties of proteases from the digestive system of the fig tree skeletonizer moth, Choreutis nemorana, were determined. Gut extracts of C.
Moloud GHOLAMZADEH CHITGAR   +2 more
doaj   +1 more source

Safety evaluation of the food enzyme containing trypsin, chymotrypsin, α‐amylase and triacylglycerol lipase from porcine pancreas

open access: yesEFSA Journal, 2022
The food enzyme complex, containing trypsin (EC 3.4.21.4), chymotrypsin (EC 3.4.21.1), α‐amylase (1,4‐α‐d‐glucan glucanohydrolase, EC 3.2.1.1) and triacylglycerol lipase (triacylglycerol acylhydrolase, EC 3.1.1.3), is obtained from porcine pancreas by ...
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +26 more
doaj   +1 more source

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