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Aspergillus oryzae enzymes

Kato, Y. and Matsuda, K. (1980) Structure of oligosaccharides obtained by controlled degradation of mung bean xyloglucan with acid and Aspergillus oryzae enzyme preparation. Agric Biol Chem 44,1751-1758... [Pg.319]

As already pointed out, the transfer reaction undergoes variation with pH similar to that of the hydrolytic reaction, so that the transfer/hy-drolysis ratio is independent of pH with coffee, lucerne, and Aspergillus oryzae enzymes. [Pg.297]

Guany 1-3,5-dimethy l-pyrazole nitrate Fungi (Mold), Yeast Amino acid oxidase, Aspergillus oryzae enzyme, Chymotrypsin,... [Pg.531]

Amino acid oxidase, Aspergillus oryzae enzyme, Chymotrypsin, Diastase, Emulsin, Hexokinase, Gluco-syltransf erase, Hog kidney enzyme, Iso-merase. Papain, Phosphatase, Pseudomonas extract Microorganisms Soil bacteria Acetobacter sub-oxydans. Streptococcus faecalis Fungi (Mold), Yeast CN-... [Pg.630]

The crystalline Aspergillus oryzae enzyme was obtained by a multistep purification produce (BIOGAL Pharmaceutical Works, Debrecen). The enzyme was electrophoretical-ly homogeneous and in anhydrous state it could be stored with unchanged activity for several years. The Ph optimum in phosphate buffer is 4.8-6.6. Its critical inactivation temperature is 65 0 and the optimal temperature 35-37 0. Specific activity 900-1000 SKE/mg protein N. The enzyme preparation contained a few percent of polysaccharide. [Pg.878]

Aspergillus oryzae Enzyme immobilized on magnetic polysilox-ane—polyvinyl alcohol 500 40 4.5 55 52 63... [Pg.659]

In all the reported examples, the enzyme selectivity was affected by the solvent used, but the stereochemical preference remained the same. However, in some specific cases it was found that it was also possible to invert the hydrolases enantioselectivity. The first report was again from iQibanov s group, which described the transesterification of the model compound (13) with n-propanol. As shown in Table 1.6, the enantiopreference of an Aspergillus oryzae protease shifted from the (l)- to the (D)-enantiomer by moving from acetonitrile to CCI4 [30]. Similar observations on the inversion of enantioselectivity by switching from one solvent to another were later reported by other authors [31]. [Pg.11]

Enzymes PPL, lipase from Pseudomonas fluorescens F-AP, lipase from Rhizopus orizae AP-6, lipase from Aspergillus niger, SP-254, lipase from Aspergillus oryzae P-2, Chirazyme WCPC, whole cell cultures of Penicillium citrinum WCPFL, whole cell cultures of Pseudomona fluorescens CAL-B, lipase from Candida antarctica B PS-C, lipase from Pseudomonas cepacia GCL, lipase from Geotrichum candidum. n.r. not reported. [Pg.175]

Fischer, brilliant results were achieved, and in succession the a-amylases of pig pancreas, of Bacillus subtilis, of human saliva, of human pancreas, and of Aspergillus oryzae, and the /3-amylase of malt, were successfully crystallized. Important biological deductions were gained from this study whereas the amylases of human pancreas and saliva cannot be distinguished from one another, amylases from pig pancreas and from human pancreas are different. These differences are manifested in molecular weight, crystalline forms, electrophoretic mobility, and influence of the pH on the activity however, all the amylases have the same specific biochemical action. The identity of the enzymes seems to be dependent on the species and not on the organ. Interest in biologically active proteins led Meyer to a study of the protein hormones, a field in which he was very active at the time of his death. [Pg.475]

Feruloyl esterase activity was first detected in culture filtrates of Strepto-myces olivochromogenes (49), and has thereafter also been reported for some hemicellulolytic fungi (Table III). A partially purified feruloyl esterase from S. commune liberated hardly any ferulic acid without the presence of xylanase (65). Very recently a feruloyl esterase was purified from Aspergillus oryzae (Tenkanen, M. Schuseil, J. Puls, J. Poutanen, K., /. Biotechnol, in press). The enzyme is an acidic monomeric protein having an isoelectric point of 3.6 and a molecular weight of 30 kDa. It has wide substrate specificity, liberating ferulic, p-coumaric, and acetic acids from steam-extracted wheat straw arabinoxylan. [Pg.431]

G. Legler and L. M. O. Osama, Mechanism of action of glycosidase splitting enzymes. IV. Purification and properties of a P-glucosidase from Aspergillus oryzae, Hoppe Seyler s Zeitschr. Physiol. Chem., 349 (1968) 1488-1492. [Pg.281]

Meat-based products have been fermented with Aspergillus in an attempt to identify novel properties. Yin et al. (2005) reported that Aspergillus oryzae produces multiple enzymes and can hydrolyze minced mackerel. The present authors (Giri et al., 2009a,b) also developed a marine fish meat-based functional paste by utilizing the traditional Japanese koji fermentation technique with improved food functionality and aroma attributes. Several trash fish, including horse mackerel, spotted mackerel, lizard fish, and squid meat, were utilized to produce a functional paste... [Pg.92]

Proteolytic enzymes derived from Aspergillus oryzae and Streptomyces griseus enhance the foaming capacity of frozen whole egg products More recently Grunden et al. ( 2) examined the... [Pg.290]


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