Results 171 to 180 of about 5,041 (212)

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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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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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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Sensitive fluorometric assay for the activity of chymosin

International Journal of Peptide and Protein Research, 1996
Fluorogenic substrates for chymosin [Dns‐Leu‐Ser‐Phe‐Trp‐Ala‐Leu‐OCH2Py (I), Dns‐Leu‐Ser‐Phe‐Met‐Trp‐Leu‐OCH2Py (II), Dns‐Leu‐Ser‐Leu‐Trp‐Ala‐Leu‐OCH2Py (III), Dns‐Leu‐Ala‐Phe‐Trp‐Ala‐Leu‐OCH2Py (IV), Dns‐Leu‐Ser‐Phe‐Leu‐Ala‐Leu‐OCH2Py (V) and Dns‐Leu‐Ser‐Phe‐Phe‐Ala‐Leu‐OCH2Py (VI)] were synthesized by a solution method.
H, Yonezawa, T, Uchikoba, M, Kaneda, N, Izumiya   +3 more
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Enzymes: Chymosin and Other Milk Coagulants

2010
The enzymatic coagulation of milk involves limited proteolysis of the caseins by enzymes in preparations called rennets, followed by aggregation of the rennet-altered casein micelles in the presence of calcium ions and at temperatures greater than ~ 18°C. In this entry, the milk protein system is reviewed briefly and the mechanism of rennet coagulation
McSweeney, P. L. H., Bansal, N.
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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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[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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Differences in the P1' substrate specificities of pepsin A and chymosin

Journal of Biochemistry, 2009
Porcine pepsin A and bovine chymosin are typical models of aspartic proteinases. The hydrolytic specificities of these proteinases, along with those of human pepsin A and monkey chymosin, were investigated with 29 peptide substrates that included various P1' variants of seven parent peptides.
Hakuto, Kageyama, Hiroshi, Ueda, Takafumi, Tezuka, Asami, Ogasawara, Yuichi, Narita, Takashi, Kageyama, Masao, Ichinose   +6 more
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Validation of Recombinant and Bovine Chymosin by Mass Spectrometry

Journal of Agricultural and Food Chemistry, 2005
Mass spectrometry has been used to map chymosin from a fermentative source. The copresence of the two known genetic variants A (Asp(244)) and B (Gly(244)) was ascertained in bovine chymosin. By contrast, either the A or the B genetic variant occurred in the three commercial samples of recombinant calf chymosin (RCC).
LILLA S, MOGNA G, ADDEO, FRANCESCO
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Fluorogenic substrates for assay of chymosin.

Biochemistry. Biokhimiia, 2000
The use of fluorogenic substrates with intramolecular fluorescence quenching as substrates for chymosin was studied. It was shown that chymosin hydrolyzes the Phe-Phe peptide bond. The effect of pH on the hydrolysis of substrates by chymosin was investigated. The catalytic characteristics of the hydrolysis of the fluorogenic substrates were obtained at
V V, Starovoitova, I Y, Filippova, E N, Lysogorskaya, E S, Oksenoit, G I, Lavrenova   +4 more
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