نتایج جستجو برای: recombinant chymosin

تعداد نتایج: 111276  

Journal: :BIO web of conferences 2023

The degree of hydrolysis and antioxidant activity protein hydrolysates from fresh cow’s milk whey obtained by the action proteolytic enzymes papain, bromelain chymosin were compared. lowest in was reported for sample MP1 (10 min reaction time, treatment with 0.1 mg/ml papain), highest percentage at hydrolysate MB12 (at 60 1.0 bromelain). For samples WC1 μl/ml chymosin), lowest. achieved WP12 us...

2012
Katarina Kosalková Carlos García-Estrada Carlos Barreiro Martha G Flórez Mohammad S Jami Miguel A Paniagua Juan F Martín

BACKGROUND The secretion of heterologous animal proteins in filamentous fungi is usually limited by bottlenecks in the vesicle-mediated secretory pathway. RESULTS Using the secretion of bovine chymosin in Aspergillus awamori as a model, we found a drastic increase (40 to 80-fold) in cells grown with casein or casein phosphopeptides (CPPs). CPPs are rich in phosphoserine, but phosphoserine its...

Journal: :Protein engineering 1998
M R Groves V Dhanaraj M Badasso P Nugent J E Pitts D J Hoover T L Blundell

In the crystal structure of uncomplexed native chymosin, the beta-hairpin at the active site, known as 'the flap', adopts a different conformation from that of other aspartic proteinases. This conformation would prevent the mode of binding of substrates/inhibitors generally found in other aspartic proteinase complexes. We now report the X-ray analysis of chymosin complexed with a reduced bond i...

Journal: :The Journal of biological chemistry 1979
B Foltmann V B Pedersen D Kauffman G Wybrandt

The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously (Pedersen, V.B., and Foltmann, B. (1975) Eur. J. Biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residu...

Journal: :Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 2005
Darío Spelzini Beatriz Farruggia Guillermo Picó

The partitioning of chymosin (from Aspergilus niger) and pepsin (from bovine stomach) was carried out in aqueous-two phase systems formed by polyethyleneglycol-potassium phosphate. The effects of polymer concentration, molecular mass and temperature were analysed. The partition was assayed at pH 7.0 in systems of polyethyleneglycol of molecular mass: 1450, 3350, 6000 and 8000. Both proteins sho...

Journal: :Biochemistry 2000
H Chen G Zhang Y Zhang Y Dong K Yang

Prochymosin (chymosin) contains three disulfide bonds: Cys45-Cys50, Cys206-Cys210, and Cys250-Cys283. We have demonstrated that Cys250-Cys283 is indispensable for correct refolding of prochymosin, whereas Cys45-Cys50 is dispensable but has some contribution to the stability and substrate specificity of the enzyme. Here, we report the results about the functions of Cys206-Cys210 by site-directed...

2004
J. WANGOH Z. FARAH

Camel milk requires more calf rennet than cow milk to coagulate and the relative amount of rennet needed varies widely (2, 8, 14, 16). Extracts of adult camel abomasa have been used to coagulate cow milk with success (5, 6, 7). However, these enzymes have not been tried on camel milk. Rennet extracts from lamb and cow calves were found to be more effective with the milk of the respective specie...

Journal: :Journal of Dairy Science 2021

In this work, pressure-assisted enzymatic gelation was applied to milk proteins, with the goal of enhancing structure and stability pressure-created protein gels. High-pressure processing (HPP) at 600 MPa, 3 min, 5°C concentrate (MPC) samples 12.5% concentration, both in absence presence calf chymosin [up 60 IMCU (international milk-clotting units)/kg milk] or camel (up 45 IMCU/kg milk). Gel ha...

Journal: :Bioscience, biotechnology, and biochemistry 2000
S Oh R W Worobo B C Kim S Rheem S Kim

The cholera toxin (CT)-binding activity of purified κ-casein macropeptide (CMP) from bovine κ-casein was detected. In addition, a statistical model was developed to optimize the production of CMP. CMP was prepared by chymosin hydrolysis of κ-casein and a subsequent 3% trichloroacetic acid treatment. CMP was further fractionated in an ion-exchange column by FPLC. CT binding activity was eluted a...

Journal: :The Biochemical journal 1977
H Keilova V Kostka J Kay

Chicken pepsinogen was incubated at pH2.5 with pepstatin. The zymogen activated itself by a sequential mechanism and an intact peptide derived from residues 1-26 in the protein was released in the first step. This peptide was found to inhibit the milk-clotting activities of pig and chicken pepsins and calf chymosin but to different extents.

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