Aspergillus saitoi

An endo-D-galacturonanase was isolated from the culture medium of Aspergillus saitoi by gel-permeation chromatography on Sepha-... 

Miyake, Y. et al., New potent antioxidative hydroxyflavanones produced with Aspergillus saitoi from flavanone glycoside in citrus fruit, Biosci. Biotechnol. Biochem., 67, 1443, 2003. 

An interesting new penta-O-substituted flavanone is 8-hydroxyhesperetin (5,7,8,3 -tetrahydroxy-4 -methoxyflavanone, 20), which was produced by the fungus Aspergillus saitoi... 

Acid Arboxypeptidase from Aspergillus Saitoi 6.1. Acid Carboxypeptidase... 

While establishing purifying for aspartic proteinase (aspergillopepsin I, EC 3.4.23.18) [7, 8] of Aspergillus saitoi, which is a food microorganism strain, it was discovered to be a rich source of acid carboxypeptidase (EC 3.4.16.5), which removes acidic, neutral, and basic amino acids as well as proline from the carboxyterminal position at pH around 3 [79, 80], The optimum pH with Z-Tyr-Leu (Z- = bebzyloxycarbonyl-) of the acid carboxypeptidase from A. saitoi was 3.5. The optimum with Z-Glu-Tyr was 3.1, and that with Z-Gly-Pro-Leu-Gly, 3.2. 

Cultivation of fungi of the genus Aspergillus is carried out both in solid ( Koji ) culture and liquid (submerged) culture. The first extracellular acid carboxypeptidase from Aspergillus saitoi was discovered by Ichishima [79], Using the method of Yphantis, the extrapolated molecular mass was determined to be 139,000 as shown in Figure 16 [79],... 

Figure 20. 400 MHz 1H-NMR spectrum of anomeric region at 50oC (A) and proposed structure (B) of the oligosaccharaide from Aspergillus saitoi carboxypeptidase.

Table 15. Kinetic parameters of active and deglycosylated acid carboxypeptidases from Aspergillus saitoi toward Z-Glu-Tyr at pH 3.1 and 30°C...

Ichishima, E. (1970). Purification and mode of assay for acid proteinase of Aspergillus saitoi. In Perlmann, G. E., and Lorand, L. (Eds.), Methods in Enzymology Proteolytic Enzymes. Vol. XIX, (pp.397-406). New York Academic Press. 

Tanaka, N., Takeuchi, M., and Ichishima, E. (1977). Purification of an acid proteinase from Aspergillus saitoi and characterization of peptide bond specificity. Biochim. Biophys. Acta, 485, 406-416. 

Gabeloteau, C., and Desnuelle, P. (1960). On the activation of beef tiypsinogen by a crystallized protease oil Aspergillus saitoi. Biochim. Biophys. Acta, 42,230-237... 

Ichishima, E., and Arai, T. (1973). Specificity and mode of action of acid carboxypeptidase from Aspergillus saitoi. Biochim. Biophys. Acta, 293, 444-450. 

Chiba, Y., Yamagata, Y., Iijima, S., Nakajima, T., and Ichishima, E. (1993). The carbohydrate moiety of the acid carboxypeptidase from Aspergillus saitoi. CurrMicrobil., 27, 281-288. 

Yamashita, K., Ichishima, E., Arai, M., and Kobata, A. (1980). An a-mannosidase purified from Aspergillus saitoi is specific for al,2 linkages. Biochem. Biophys. Res.Commun., 96, 1335-1342. 

Ichishima, E., Taya, N., Ikeguchi, M., Chiba, Y., Nakamura, M., Kawabata, C., Inoue, T., Takahashi, K., Minetoki, T., Ozeki, K., Kumagai, C., Gomi, K., Yoshida, T., and Nakajima, T. (1994). Molecular and enzymatic properties of recombinant 1,2-a-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells. Biochem. J., 339, 589-597. 

Fujita, A., Yoshida, T., and Ichishima, E. (1997). Five crucial carboxyl residues of 1,2-a-D-mannosidase from Aspergillus saitoi (A. phoenicis), a food microorganism, are identical by site-directed mutagenesis. Biochem. Biophys. Res. Commun., 238, 779-783. 

Aspergillopeptidase A (E.C. 3.4.4.17) is an acid proteinase from Aspergillus saitoi. This enzyme may be prepared and assayed by the procedures described by E. Ichishima, Methods Enzymol. 19, 397 (1970). 

Esaki, H., Watanabe, R., Onozaki, H., Kawakishi, S., and Osawa, T. 1999. Formation mechanism for potent antioxidative o-dihydroxyisoflavones in soybeans fermented with Aspergillus saitoi. Biosci. Biotech. Biochem. 63 851-858. 

Protease from Aspergillus saitoi Protease from Bacillus subtilis Protease from Aspergillus oryzae Protease from Streptomyces griseus... 

Two other proteases have been commercialized by Sigma and used for such experiments. They both are extracts from fungi protease from. Rhizopus species (type XVIII), EC 3.4.23.6, optimum pH 3 and protease from Aspergillus saitoi (type XIII), EC 3.4.23.18, optimum pH 2.8. Several others were purified or overexpressed by groups developing the approach. 

Type XIII Aspergillus saitoi P H, E, R, K, E Crude culture extract... 

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