Results 211 to 220 of about 7,296 (278)

The crystallography of calf rennin (chymosin)

Proceedings of the Royal Society of London. Series B. Biological Sciences, 1971
The growth of crystals of calf rennin (chymosin, † EC 3.4.4.3) and the control of nucleation to produce crystals of desired size, are described. Only one stable species, orthorhombic rennin I, has been found, but a metastable monoclinic species, rennin II, appeared on one occasion in a solution nearly saturated with glycine.
C W, Bunn, P C, Moews, M E, Baumber
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Increased production of chymosin by glycosylation

Journal of Biotechnology, 2006
Filamentous fungi are well known in the industry as producers of large amounts of extracellular proteins. However, production levels of heterologous proteins are often disappointing low. In this paper it is shown that increasing glycosylation is a powerful strategy for increasing production levels of chymosin in filamentous fungi.
Hans J M, van den Brink, Steen Guldager, Petersen, Henrik, Rahbek-Nielsen, Karsten, Hellmuth, Marianne, Harboe   +4 more
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Thermal inactivation of chymosin during cheese manufacture

Journal of Dairy Research, 2002
The aspartic proteinase, chymosin (EC 3.4.23.4) is the principal milk clotting enzyme used in cheese production and is one of the principal proteolytic agents involved in cheese ripening. Varietal differences in chymosin activity, due to factors such as cheese cooking temperature, fundamentally influence cheese characteristics.
Maurice G, Hayes, Jorge C, Oliveira, Paul L H, Mcsweeney, Alan L, Kelly   +3 more
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Commercial Levels of Chymosin Production by Aspergillus

Bio/Technology, 1991
We have increased the production of bovine chymosin in Aspergillus niger var. awamori to more than one gram per liter of secreted authentic enzyme by combining a mutagenesis protocol with a novel robotic screening program. Analysis of the superior chymosin producing strains indicated that they have enhanced capabilities to secrete extracellular ...
Nigel S. Dunn-Coleman, Peggy Bloebaum, Randy M. Berka, Elizabeth Bodie, Nancy Robinson, Gale Armstrong, Michael Ward, Melinda Przetak, Gina L. Carter, Regina LaCost, Lori J. Wilson, Katherine H. Kodama, Enrique F. Baliu, Ben Bower, Michael Lamsa, Henry Heinsohn   +15 more
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Codon Optimization of the “Bos Taurus Chymosin” Gene for the Production of Recombinant Chymosin in Pichia pastoris

Molecular Biotechnology, 2016
Codon optimization of the Bos taurus Chymosin gene (CYM) for its expression in Pichia pastoris was performed in this study. A synthetic CYM gene was designed in silico by replacing codons rarely used by P. pastoris with equivalent nucleotide combinations that codify for the same amino acid but that are more frequently encountered in the genome of P ...
Jose Alberto, Espinoza-Molina, Carlos Horacio, Acosta-Muñiz, D R, Sepulveda, Paul Baruk, Zamudio-Flores, Claudio, Rios-Velasco   +4 more
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Stimulation of chymosin secretion by simultaneous expression with chymosin-binding llama single-domain antibody fragments in yeast

Applied Microbiology and Biotechnology, 2002
We studied the effect of coexpression of chymosin and chymosin-binding llama single-domain antibody fragments (VHHs) on the secretion of chymosin by Saccharomyces cerevisiae cells. A VHH expression library containing chymosin-specific VHHs was obtained by immunization of a llama and coexpressed with chymosin in yeast. From this library, we obtained two
Harmsen, M.M., Smits, C.B., de Geus, B.
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Chymosin-catalyzed peptide synthesis.

Biomedica biochimica acta, 1992
Calf chymosin catalyzes peptide synthesis optimally at pH 4-5 giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexapeptides, provided that hydrophobic amino acid residues form the new peptide bond. The enzyme efficiency depends also on the nature of adjacent amino acid residues.
C A, Abdel Malak, G I, Lavrenova
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[Biospecific chromatography of chymosin].

Biokhimiia (Moscow, Russia), 1976
Chromatography of commercial rennet was studied on biospecific sorbents obtained by means of coupling of activated Sepharose 4B with epsilon-aminocapronyl-D-phenylalanine methyl ester and amide, epsilon-aminocapronyl-L-phenylalanyl-D-phenylalanine methyl ester, gramicidin S and N-2,4-dinitrophenylhexamethylenediamine.
V M, Stepanov, G I, Lavrenkova, K, Adli, M V, Gonchar, G N, Balandina   +4 more
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INFLUENCE of ULTRASOUND ON the PROPERTIES of CHYMOSIN and the ULTRASTRUCTURE of ABOMASUM DURING CHYMOSIN EXTRACTION

Journal of Food Processing and Preservation, 1991
The effects of ultrasound treatment on the properties of chymosin and the ultrastructure of abomasum during chymosin extraction were investigated. Ultrasound treatment at 36 W/cm2 for 80 min did not decrease chymosin activity and its proteolytic activity.
S. M. KIM, J. F. ZAYAS
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The Presence of Chymosin Inhibitor in Seminal Plasma

Zentralblatt für Veterinärmedizin Reihe A, 1983
SummaryDetermination of chymosin, an acid protease, as assessed by the turbidimetric method and by the glycomacropeptide release method, showed that cattle seminal plasma inhibits this enzyme's action on milk and on K‐casein. Fractionation of the proteins present in the seminal plasma by gel filtration on Sephadex G‐10 resulted in its resolution into ...
P, Palta, N C, Ganguli
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