Aspergillus oryzae enzyme from

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]. 

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. 

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. 

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. 

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. 

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... 

Leucine aminopeptidase may be isolated from Aspergillus oryzae.1300 The RMM (37 500) of this enzyme is significantly smaller than that from mammalian sources, but, like the latter, it is a metalloenzyme. 

Bovine pancreatic RNase A is a member of a homologous superfamily. In addition, there is a separate family of guanine-specific microbial RNases that have evolved to have a similar active site.192,193 Ribonuclease T1 from Aspergillus oryzae and the 110-residue bamase from Bacillus amyloliquefaciens of Mr 12 392 (see Chapter 19) are the best known examples. One of the histidine residues is replaced by a glutamate in these enzymes. The microbial enzymes are much more amenable to study by protein engineering. 

The most important features are, first, that some of the a-amylases— i.e., those in digests Numbers 4, 5, 6, and 7 have catalyzed glycosylations from a-maltosyl fluoride at one-tenth to one-one hundredth the enzyme concentrations required for action on a-D-glucosyl fluoride. The Aspergillus oryzae a-amylase, which had the weakest synthetic action on a-D-glucosyl fluoride of the enzymes tested at 100 ftg/ml, has produced under conditions of this experiment an extended series of maltosaccharides at 1 fig/ml. 

Of the two homogeneous preparations of a nonspecific adenosine aminohydrolase from Aspergillus oryzae (Takadiastase) (92,179), that described by Wolfenden et al. (92) appears to be more facile and concise. Both procedures yield enzyme with turnover numbers near 105 moles adenosine deaminated per minute and molecular weights near 215,000. The mo-... 

In 1957, RNase T, (5, 10, 11) was isolated from Takadiastase, a commercial product of Aspergillus oryzae (12). It is now a familiar enzyme used as an essential tool for the structural analysis of RNA. 

An even more serious disadvantage of this technique is that it often impairs the biological activity of the modified protein. The activities of hen s egg lysozyme (EC 3.2.1.17) and alpha amylase from Aspergillus oryzae (EC 3.2.1.1) were lessened by diazo coupling of glycosides or aniline.12 Whether the decrease in activity was due to the modification of critical residues, or to the introduction of aromatic structures, is not yet clear however, enzymes subjected to the diazocoupling conditions in the absence of the diazonium salts retained their activity, implying that the reaction conditions themselves were not responsible for the loss of activity. 

Acylase (acylase I aminoacylase N-acetyl amino acid amidohydrolase E.C. 3.5.1.14), is one of the best-known enzymes as far as substrate specificity (Chenault, 1989) or use in immobilized (Takahashi, 1989) or membrane reactors (Wandrey, 1977, 1979 Leuchtenberger, 1984 Bommarius, 1992a) is concerned however, its exact mechanism or 3D structure is still not known (Gentzen, 1979 1980). Acylase is available in large, process-scale quantities from two sources, porcine kidney and the mold Aspergillus oryzae. 

I. Gentzen, H.-G. Loffler, and F. Schneider, Aminoacylase from Aspergillus oryzae. Comparison with the pig kidney enzyme, Z. Naturforsch. 1980, 35c, 544-550. 

Similarly, in 1952, Pazur reported61 that a fungal enzyme from Aspergillus oryzae is capable of transferring D-fructose residues from one molecule of raffinose to another, to give a new tetrasaccharide and a new pentasaccharide. 

Lacto-N-triose IPK is split (by the /3-A7-acetylglucosaminidase from Aspergillus oryzae) into 2-acetamido-2-deoxy-D-glucose plus lactose, which would be expected on the basis of the structure proposed. Lacto-iV-triose I is unaffected by this enzyme. 

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