Results 221 to 230 of about 13,591 (265)

Decoding the functional plasticity of milk-derived exosomes: implications for nutrition, immunity, and therapy. [PDF]

open access: yesFront Immunol
Hussain S   +9 more
europepmc   +1 more source

Tailored collagen binding of albumin-fused hyperactive coagulation factor IX dictates in vivo distribution and functional properties. [PDF]

open access: yesNat Commun
Aaen KH   +15 more
europepmc   +1 more source

Purified zymogens reveal mechanisms of snake venom metalloproteinase auto-activation. [PDF]

open access: yesElife
Hall S   +17 more
europepmc   +1 more source

High-Level Expression and Substrate-Binding Region Modification of a Novel BL312 Milk-Clotting Enzyme To Enhance the Ratio of Milk-Clotting Activity to Proteolytic Activity

open access: yesJournal of Agricultural and Food Chemistry, 2019
A novel BL312 milk-clotting enzyme (MCE) exhibited high-level expression and remarkable milk-clotting activity (MCA) (865 ± 20 SU/mL) that was 3.3-fold higher than the control by optimizing induction conditions in recombinant Escherichia. coli harboring pET24a-proMCE.
Yao Zhang   +2 more
exaly   +4 more sources

Measurement of milk clotting activity by rotational viscometry

open access: yesJournal of Dairy Research, 2011
Standard method for the determination of the activity of milk coagulants is the rotating bottle method, where clotting time is defined as the time when visually observable flocculation starts. Aim of this study was to verify whether it is possible to determine milk clotting time by rotational viscometry.
Mandy, Jacob   +3 more
openaire   +3 more sources
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Milk-clotting activity of cucumisin, a plant serine protease from melon fruit

Applied Biochemistry and Biotechnology, 1996
Cucumisin (EC 3.4.21.25) isolated from prince melon fruit is a plant serine protease. Its milk-clotting activity was compared with plant cysteine proteases such as papain (EC 3.4.22.2) and ficain (EC 3.4.22.3). Cucumisin was more stable than papain under the condition of pH 7.1, 37 degrees C for 24 h.
Tetsuya Uchikoba   +2 more
exaly   +3 more sources

Proteolytic and milk clotting activities in extracts obtained from the crustaceans Munida

open access: yesJournal of Molecular Catalysis B: Enzymatic, 2003
Abstract In the present study, individuals of the crustaceans Munida have been investigated as a possible source of enzymes to be used in cheese making as an alternative to calf rennet. The crustaceans were blended and the extracts were filtered and tested for their proteolytic activity and milk clotting capability.
DAMBROSIO A   +3 more
openaire   +3 more sources

Immunochemical, chromatographic, and milk-clotting activity measurements for quantification of milk-clotting enzymes in bovine rennets

Journal of Dairy Research, 1976
SummaryMonospecific rabbit antibodies were produced against bovine chymosin (rennin) and bovine pepsin A and used for quantitative measurements of these enzymes by rocket immunoelectrophoresis. Bovine pepsin B was identified and measured quantitatively in tandem crossed immunoelectrophoresis, using a polyspecific antibody preparation ...
G A, Rothe   +3 more
openaire   +2 more sources

Activity and Properties of the Penicillium citrinum Milk-clotting Enzyme

Zentralblatt für Bakteriologie, Parasitenkunde, Infektionskrankheiten und Hygiene. Zweite Naturwissenschaftliche Abteilung: Allgemeine, Landwirtschaftliche und Technische Mikrobiologie, 1974
Summary In the presence of substrate, the milk-clotting enzyme preparation of Penicillium citrinum showed a good stability against heat and p H changes. A linear relationship was observed between the amount of the enzyme and the reciprocal of clotting time. The rate of milk-clotting depended on a certain ratio between the enzyme and the substrate.
A F, Abdel-Fattah, N M, El-Hawwary
openaire   +2 more sources

Milk-clotting activity of proteinases produced by Rhizopus

Canadian Journal of Microbiology, 1969
Rhizopus oligosporus NRRL 3271 produces an enzyme having high milk-clotting activity. High yields of the enzyme were noted in the culture filtrates of milk, wheat flour, or wheat bran. The enzyme was stable at 40 °C, or below, but its activity was destroyed rapidly by heating at 60 °C.
H L, Wang, D I, Ruttle, C W, Hesseltine
openaire   +2 more sources

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