Results 31 to 40 of about 111,709 (349)

Cys25‐nitrosylation inactivates papain [PDF]

open access: yesIUBMB Life, 1998
AbstractNitric oxide (NO) may modulate the catalytic activity of cysteine proteases. In the present study, the inhibitory effect of NO, released by the NO‐donors (±)‐(E)‐4‐ethyl‐2‐[(E)‐hydroxyimino]‐5‐nitro‐3‐hexenamide and nitroprusside, on papain action is reported.
VENTURINI G   +4 more
openaire   +5 more sources

A study of the enzymatic hydrolysis of fish frames using model systems [PDF]

open access: yes, 2011
A model system was employed to study the operating conditions and primary parameters of enzymic hydrolysis of cod proteins. Pancreatin, papain, and bromelain were used to hydrolyse minced cod fillets under controlled conditions and with the rate of ...
Himonides, Aristotelis T.   +2 more
core   +1 more source

Peptide synthesis by recombinant Fasciola hepatica cathepsin L1 [PDF]

open access: yes, 2006
Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0–12.5%
Ciarán Ó'Fágáin   +16 more
core   +1 more source

Production and Characterization of Antioxidative Hydrolysates and Peptides from Corn Gluten Meal Using Papain, Ficin, and Bromelain

open access: yesMolecules, 2020
There has been a growing interest in developing natural antioxidants with high efficiency and low cost. Bioactive protein hydrolysates could be a potential source of natural and safer antioxidants.
Ruijia Hu, Gengjun Chen, Yonghui Li
semanticscholar   +1 more source

Allosteric Inhibition of Factor XIIIa. Non-Saccharide Glycosaminoglycan Mimetics, but Not Glycosaminoglycans, Exhibit Promising Inhibition Profile [PDF]

open access: yes, 2016
Factor XIIIa (FXIIIa) is a transglutaminase that catalyzes the last step in the coagulation process. Orthostery is the only approach that has been exploited to design FXIIIa inhibitors.
Afosa, Daniel K.   +4 more
core   +4 more sources

Safety evaluation of the food enzyme papain, a cysteine endopeptidase complex from the latex of <i>Carica papaya</i> L. [PDF]

open access: yesEFSA J
Abstract The food enzyme is a cysteine endopeptidase complex, containing papain (EC 3.4.22.2), chymopapain (EC 3.4.22.6), caricain (EC 3.4.22.30) and glycyl endopeptidase (EC 3.4.22.25), obtained from the latex of unripe Carica papaya L. by Enzybel International SA. It is intended to be used in nine food manufacturing processes.
EFSA Panel on Food Enzymes (FEZ)   +16 more
europepmc   +4 more sources

THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN

open access: yesThe Journal of General Physiology, 1938
In the hemoglobin method for the estimation of proteinase, denatured hemoglobin is digested under standard conditions, the undigested hemoglobin is precipitated with trichloracetic acid, and the amount of unprecipitated protein split products, which is a
M. L. Anson
semanticscholar   +1 more source

High Molecular Weight Silk Fibroin Prepared by Papain Degumming

open access: yesPolymers, 2020
A major challenge for the silk textile industry and for the process of silk-based biomaterials is to find a degumming method that can completely remove sericin while avoiding obvious hydrolysis damage to the silk fibroin.
Yanfei Feng   +6 more
semanticscholar   +1 more source

Penghambatan Enzim Pemecah Protein (Enzim Papain) Oleh Ekstrak Rokok, Minuman Beralkohol Dan Kopi Secara In Vitro

open access: yesJurnal Kimia Valensi, 2012
Telah dilakukan penelitian tentang pengaruh ekstrak rokok, kopi dan minuman beralkohol terhadap aktivitas enzim papain.  Tujuan penelitian ini untuk mengetahui pengaruh ekstrak rokok, kopi dan minuman beralkohol terhadap aktivitas enzim pencernaan ...
La Ode Sumarlin   +2 more
doaj   +1 more source

Solution structure of a phytocystatin from Ananas comosus and its molecular interaction with papain. [PDF]

open access: yesPLoS ONE, 2012
The structure of a recombinant pineapple cystatin (AcCYS) was determined by NMR with the RMSD of backbone and heavy atoms of twenty lowest energy structures of 0.56 and 1.11 Å, respectively.
Deli Irene   +7 more
doaj   +1 more source

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