Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Zahid Mozaffar"'
Publikováno v:
Canadian Journal of Microbiology. 42:1241-1247
Isocitrate dehydrogenase is considered to be one of the key regulatory enzymes in the conversion of glucose into fatty acids by oleaginous microorganisms. A dual coenzyme-specific isocitrate dehydrogenase (EC 1.1.1.41) (IDH) was isolated from the pri
Autor:
John D. Weete, Zahid Mozaffar
Publikováno v:
Journal of the American Oil Chemists' Society. 72:1361-1366
An extracellular lipase from the fungusPythium ultimum was active in an invert [water-in-oil] emulsion consisting of 4% water emulsified into edible oils with taurocholic acid as the surfactant. The pH range for optimum lipolytic activity was 7.5–8
Autor:
Zahid Mozaffar, Zahur U. Haque
Publikováno v:
Food Hydrocolloids. 5:559-571
Acid casein was continuously modified using immobilized (IM-) trypsin, chymotrypsin and Rhozyme-41. The objective was bulk production of hydrolysates with desirable functional attributes. The degree of modification was controlled by regulating the fl
Autor:
Zahur U. Haque, Zahid Mozaffar
Publikováno v:
Food Hydrocolloids. 5:549-557
Proteolytic enzymes were immobilized onto suitable carriers with the objective of standardizing stable immobilized-enzyme (IME) bioreactors to hydrolyze casein continuously. Papain, trypsin, chymotrypsin, pancreatin, Rhozyme-41, chymosin, plasmin and
Autor:
Zahur U. Haque, Zahid Mozaffar
Publikováno v:
Food Hydrocolloids. 5:573-579
Two different kinds of ‘plastein type’ peptide preparations, one dispersible (yield 97%, w/w of total casein) and the other indispersible (yield 3% w/w of total casein) in water, were synthesized by treating casein hydrolysate with papain. These
Autor:
Zahur U. Haque, Zahid Mozaffar
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 57:689-690
Publikováno v:
Journal of Food Science. 50:1602-1606
The characteristics of β-galactosidase from Bacillus circulans, and its suitability for hydrolysis of milk lactose were compared with those of Escherichia coli and Kluyveromyces lactis enzymes. Enzyme activity of β-galactosidase from B. circulans w
Publikováno v:
Agricultural and Biological Chemistry. 48:3053-3061
βS-Galactosidases (EC 3.2.1.23) from Bacillus circulans were purified and separated into two different enzyme forms, using Sephadex G-150, ion-exchange, polybuffer chromatography, and preparative polyacrylamide gel electrophoresis. The molecular wei
Publikováno v:
Biotechnology Letters. 10:805-808
The oligosaccharide-producing activity of beta-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1. 23) preparation ofBacilluscirculans was increased from 21% to 40% after glutaraldehyde treatment or immobilization onto porous silicagel(Merc
Publikováno v:
Agricultural and Biological Chemistry. 48:3053-3061