Results 171 to 180 of about 51,627 (231)

Sustainable reactive dyeing of polyester/cotton blend fabric via papain enzyme surface modification. [PDF]

Sci Rep
Molla WT, Kebede Z, Semagn N, Adgo A, Godana C.   +4 more
europepmc   +1 more source

Ultrasound-assisted enzymatic modification: An approach to enhance the quality and functionality of camel milk hydrolysates. [PDF]

Ultrason Sonochem
Tanwar A, Kumar Y, Berwal R, Harsh A, Priyadarsini S, Bumbadiya M.   +5 more
europepmc   +1 more source

Thermo- and pH-Responsive Antimicrobial Hydrogels from Poly(2-(dimethylamino)ethyl methacrylate) and Cationic-Modified Chitosan for Sustained Papain Release. [PDF]

ACS Polym Au
Ferreira CC, Schutz GF, Carmo IAD, Teixeira LN, Martinez EF, Mei LHI, Vieira RP.   +6 more
europepmc   +1 more source

Preparation of Antioxidant Peptides Derived From Quinoa Protein and Evaluation of Their Antioxidant Activity Through a D-Galactose-Induced Aging Mice Model. [PDF]

Food Sci Nutr
Gao D, Zhang Y, Ma H.
europepmc   +1 more source

Rigor & Reproducibility: pH Adjustments of Papain with L-Cysteine Dissociation Solutions and Cell Media Using Phenol Red Spectrophotometry. [PDF]

Biosensors (Basel)
Hilner JM, Turner A, Vollmar-Zygarlenski C, Millet LJ.   +3 more
europepmc   +1 more source

Preparation, allergenicity analysis and nutritional evaluation of partially and extensively hydrolyzed whey protein peptides. [PDF]

NPJ Sci Food
Zheng S, Zhang R, Chen X, Du M, Li H, Wang J, Sun B.   +6 more
europepmc   +1 more source

Proteolytic enzyme models as tunable preclinical platforms for investigating intervertebral disc degeneration. [PDF]

Front Cell Dev Biol
Gewiess J, D'Intino A, Santos A, Alini M, Vernengo AJ.   +4 more
europepmc   +1 more source

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Structure of Papain

Nature, 1968
A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft. The active site, consisting of a cysteine and a histidine, lies at the surface of the cleft. Apart from four short α-helical segments and one short segment of β-structure,
J, Drenth, J N, Jansonius, R, Koekoek, H M, Swen, B G, Wolthers   +4 more
openaire   +2 more sources

Thiirancarboxamides as Inhibitors of Papain

Archiv der Pharmazie, 2004
AbstractDerivatives of the thiirancarboxylic acid building‐block containing a peptide bond were synthesised and screened against the model cysteine protease papain. The most active of the series showed a second‐order rate constant of inactivation comparable to that of the parent compound.
Gemma, Bruno, Tanja, Schirmeister
openaire   +2 more sources