نتایج جستجو برای: recombinant chymosin

تعداد نتایج: 111276  

Journal: :Antimicrobial agents and chemotherapy 1997
K S Hoek J M Milne P A Grieve D A Dionysius R Smith

Several peptides sharing high sequence homology with lactoferricin B (Lf-cin B) were generated from bovine lactoferrin (Lf) with recombinant chymosin. Two peptides were copurified, one identical to Lf-cin B and another differing from Lf-cin B by the inclusion of a C-terminal alanine (lactoferricin). Two other peptides were copurified from chymosin-hydrolyzed Lf, one differing from Lf-cin B by t...

Journal: :The Biochemical journal 1992
C A Abdel Malak

Calf chymosin was shown to catalyse peptide synthesis optimally over the range pH 4-5, giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino-acid residues form the new peptide bonds. The effectiveness of the enzyme depends also on the nature of adjacent amino-acid residues. As an aspartate-proteinase with a c...

Journal: :The Biochemical journal 1978
B Foltmann P Lønblad N H Axelsen

The stomach of newborn pig contains a proteinase that is immunologically closely related to calf chymosin (rennin) (EC 3.4.23.4.). None of the pepsins from the stomach of adult pig is present in the newborn pig. Pig chymosin has optimal general proteolytic activity around pH 3.5. The ratio of milk-clotting activity to general proteolytic activity is about 30--70 times higher than that of pylori...

Journal: :Biotechnology progress 1992
A Carlson R Nagarajan

After complete solubilization by the direct method, porcine pepsin was not released from AOT in isooctane reverse micelles even under aqueous-phase conditions which would not ordinarily allow uptake. Similarly, bovine chymosin, once forward-transferred at a pH below its isoelectric point, was not back-transferred into an aqueous contact phase buffered at a pH value above its isoelectric point. ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1983
J S Emtage S Angal M T Doel T J Harris B Jenkins G Lilley P A Lowe

A gene for calf prochymosin (prorennin) has been reconstructed from chemically synthesized oligodeoxyribonucleotides and cloned DNA copies of preprochymosin mRNA. This gene has been inserted into a bacterial expression plasmid containing the Escherichia coli tryptophan promoter and a bacterial ribosome binding site. Induction of transcription from the tryptophan promoter results in prochymosin ...

Journal: :Journal of Dairy Science 2021

Chymosin is a predominant enzyme in rennet and used cheese production because of its excellent milk-clotting activity. Herein, we proposed facile label-free electrochemical method for determining chymosin activity based on peptide-based substrate. The synthesized substrate peptide was assembled onto the surface Au-deposited grassy carbon electrode. current proportional to activity, thus could b...

Journal: :Hoppe-Seyler´s Zeitschrift für physiologische Chemie 1908

Journal: :Biochemical Society transactions 1991
R M Berka K H Kodama M W Rey L J Wilson M Ward

Filamentous fungi possess unique features which make them attractive as hosts for the production of heterologous gene products. For example, certain fungal species are capable of secreting large quantities of protein in submerged culture. Selected strains of Aspergillus niger can produce greater than 20 g of glucoamylase I ~ I in industrial fermentations [ 11. Some filamentous fungi, including ...

2015
Mehmet Çelebi Bedia Şimşek

In this study, Örgü cheese has been produced by using different coagulating enzymes (calf rennet, microbial enzymes, recombinant chymosin). The effects of different coagulating enzymes which are used on the characteristic of mineral material and cheese has been observed during 90 days ripening time. Mineral material contents of Örgü cheese have been determined with ICP-OES (inductively coupled ...

Journal: :Journal of dairy science 2015
H Eshpari R Jimenez-Flores P S Tong M Corredig

Milk protein concentrate powders (MPC) with improved rehydration properties are often manufactured using processing steps, such as acidification and high-pressure processing, and with addition of other ingredients, such as sodium chloride, during their production. These steps are known to increase the amount of serum caseins or modify the mineral equilibrium, hence improving solubility of the r...

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