Results 201 to 210 of about 12,767 (243)

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
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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
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Proteolytic activities of some milk clotting enzymes on ovine casein

Food Chemistry, 2000
Proteolytic activity of some milk clotting enzymes (calf and lamb rennets, bovine chymosin and pepsin, and proteases from Rhizomucor miehei and Cryphonectria parasitica) on ovine whole casein was determined by urea-PAGE and RP-HPLC. Microbial enzymes were more proteolytic than animal enzymes when acting on ovine whole casein.
Antonio J. Trujillo, Buenaventura Guamis, José Laencina, Marı́a B. López   +3 more
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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.
T, Uchikoba, M, Kaneda
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Production of highly active fungal milk-clotting enzyme by solid-state fermentation

Preparative Biochemistry & Biotechnology, 2019
Cheese production is projected to reach 20 million metric tons by 2020, of which 33% is being produced using calf rennet (EC 3.4.23.4). There is shortage of calf rennet, and use of plant and microbial rennets, hydrolyze milk proteins non-specifically resulting in low curd yields.
Cirium V. Chinmayee, Cheral Vidya, Amsaraj Rani, Sridevi Annapurna Singh   +3 more
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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

Journal 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, Yongjun Xia, Xiaofeng Liu, Zhiqiang Xiong, Shijie Wang, Na Zhang, Lianzhong Ai   +6 more
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Proteolytic and milk clotting activities in extracts obtained from the crustaceans Munida

Journal 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, UNGARO N, ROSSANO, Rocco, RICCIO, Paolo   +3 more
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Site-specific mutations of calf chymosin B which influence milk-clotting activity

Food Chemistry, 1998
Abstract Zymogen forms of wild type and three mutant calf chymosin B enzymes were heterologously expressed in Escherichia coli under control of a T7 promoter as inclusion bodies. The chaperone-like protein, α-crystallin, was used as a possible aid to unfolding.
Supannee Chitpinityol, Derek Goode, M.James C. Crabbe   +2 more
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Comparison of total milk-clotting activity measurement precision using the Berridge clotting time method and a proposed optical method

Journal of Food Engineering, 2012
Abstract An objective measurement technique is needed to simplify the determination of total milk-clotting activity (at) of rennets and other milk coagulating enzymes. IDF Standard 157: 2007 /ISO 11815 is the current standard method for bovine rennets and measures milk-clotting activity by visually determining the Berridge clotting time (i.e., time ...
N. Tabayehnejad, M. Castillo, F.A. Payne
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Comparative Study of Proteolytic Activities of Some Commercial Milk Clotting Enzymes on Bovine Skim Milk

Journal of Animal Science and Technology, 2002
Proteolytic activities of some commercial milk clotting enzymes(rennet, trypsin, pepsin, papain W-40, neutrase 1.5 and protease S) in bovine skim milk containing 0.02% were determined by measuring DH(Degree of Hydrolysis), NPN(Non Protein Nitrogen) and by comparing patterns of SDS-PAGE(Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis). The DH
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