Results 181 to 190 of about 51,553 (242)

Effects of papain enzymolysis on the functional properties, stability and sensory quality of soy milk after thermal steam treatment. [PDF]

Food Chem X
Sun F, Jin Y, Liu M, Zhou L, Sun Y, Han C, Guo Z, Liu Y, Wang Z.   +8 more
europepmc   +1 more source

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

Impact of Plant and Microbial Proteases Treatment on Quality Characteristics of Beef <i>Longissimus Thoracis</i> and <i>Lumborum</i>. [PDF]

Food Sci Anim Resour
Akkaya E, Bingol EB, Hampikyan H, Colak H.   +3 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

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