Unique Enzymes of Aspergillus Fungi Used in Japanese by Eiji Ichishima
By Eiji Ichishima
The main everyday organisms are fungi, and several other enzymes and natural acids are synthesized via species of Aspergillus. over the last 1,000 years, using hydrolytic enzymes from fungi has turn into extra familiar in jap fermentation industries. The molds Aspergillus oryzae, A. sojae, A. awamori and A. saitoi are of serious useful significance in fermentation industries, enzyme applied sciences and nutrients industries in Japan. This booklet discusses the catalytic and molecular homes of specific and attribute enzymes got from Aspergillus fungi utilized in eastern bioindustries.
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Extra resources for Unique Enzymes of Aspergillus Fungi Used in Japanese Bioindustries
Sample text
Consequently the enzyme activity of the transformant was observed to be about 10-fold 32 Eiji Ichishima higher than that of the recipient strain in the solid culture, but neither demonstrated any activity in the submerged culture. This finding indicates that the cloned gene is functional and expressed only in the solid culture state. A 4 kb XbaI fragment of the cloned aorO gene and cDNA were sequenced and compared. Eight introns with short sequences of 50-75 nucleotides were found in the gene. The complete structural gene encoded a protein of 652 amino acids.
Yamaguchi, M. , Phytochemistry, 33, 1317-1321 (1993)) 44 Eiji Ichishima Table 10. Secondary structure content (%) in penicillolysin, apoenzyme and Co2+-penicillolysin Enzyme α-Helix β-Structure Turn Penicillolysin 19 58 3 Apoenzyme 9 61 2 Co2+20 58 2 penicillolysin (Yamaguchi, M. , Phytochemistry, 33, 1317-1321 (1993)) Random 21 28 20 A full-length cDNA encoding the penicillolysin, an 18 kDa metalloendopeptidase from Penicillium citrinum, was cloned [70]. Analysis of the 1284 base pair nucleotide sequence of the cDNA revealed a single open reading frame coding for 351 amino acid residues.
The pH-dependent changes of substrate preference are shown in Figure 8. The P1 Lys/Phe preference increased as pH rose, which indicates that the dissociation of a carboxyl group as Asp77 may affect the preference of a Lys residue at the P1 position. Figure7. pH dependence of pKm. logkcat, amd log(kcat/Km) for hydrolysis of Pro-ThrGlu-Phe-Phe(NO2)-Arg-Leu (●), Pro-Thr-Glu-Lys-Phe(NO2)-Arg-Leu (○), and AcAla-Ala-Lys-Phe(NO2)-Ala-Ala-NH2 (▲) by T77D/G78(S)S79 mutant pepsins. (Shintani, T. , J. Biol.



