Detail of "988-75-0"

Reference

Selective breeding of high peptidase-producing Aspergillus oryzae strains

Selective breeding of high peptidase-producing Aspergillus oryzae strains. I. Determination of enzymes and screening of microbial strains. Sun, Jinfang; Li, Ruilian; Wang, Xiaolian; Jiang, Qingyan (Heilungjiang Inst. Appl. Microbiol., Peop. Rep. China). Zhongguo Tiaoweipin, (8), 24-6 (Chinese) 1984. CODEN: ZHTIE7. DOCUMENT TYPE: Journal CA Section: 16 (Fermentation and Bioindustrial Chemistry) Proteinase [9001-92-7] and peptidase [9031-96-3], including aminopeptidase [9031-94-1] and carboxypeptidase [9031-98-5] activities, were detected in various A. oryzae strains using casein (proteinase), DL-Leu-Gly-Gly [4337-37-5] or L-Leu-b-naphthylamine [732-85-4] (aminopeptidase), and Cbz-Glu-Tyr [988-75-0] (carboxypeptidase) as substrates to screen A. oryzae strains for soy sauce prodn. Most of the screened strains contained high proteinase and low peptidase activity. There was an 8-fold interstrain variation in proteinase content and a 4-fold interstrain variation in peptidase contents. Proteinase prodn. was related to the growth rate and spore count; the proteinase yield was high in strains with low growth rate and low spore count, and was high in strains with high growth rate and spore count. In contrast, the peptidase yield was not related to growth and spore count. There was no correlation between proteinase and peptidase activities. These tested peptidase substrates also showed strain variations, suggesting that a more effective method must be developed for screening of peptidase-producing A. oryzae strains.

Partial purification and some enzymic properties of cathepsin A (F-II) from squid liver

Partial purification and some enzymic properties of cathepsin A (F-II) from squid liver. Ikeda, Eiko; Inaba, Takashi; Fujii, Minoru (Lab. Biochem., Saga Univ., Saga, Japan). Saga Daigaku Nogaku Iho, 41, 9-20 (Japanese) 1976. CODEN: SDNIA4. 988-75-0 and 987-84-8 are also occured in this study. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Cathepsin A from the liver of squid, Dorytheuthis bleederi, was sepd. into 2 active fractions, F-I and F-II, by CM-cellulose column chromatog. F-II was partially purified .apprx.100-fold. Gel filtration on Sephadex g-200 gave mol. wts. of .apprx.107,000 and 58,000 for F-I and F-II, resp. Isoelec. focusing of F-II gave an isoelec. point of pH 5.1. The enzyme was stable between pH 4.9-5.6. The optimum pH for the hydrolysis of Z-Glu-Tyr (Z = N-carbobenzoxy) was 4.6-5.2. The enzyme catalyzed the hydrolysis of dipeptide derivs., such as Z-Glu-Tyr, Z-Glu-Phe, and Z-Gly-Phe. Z-Gly-Leu and Z-Gly-Pro were hardly hydrolyzed. The values of Km for Z-Gly-Tyr and Z-Glu-Phe were 1.5 and 3.2 mM, resp., in 0.1M acetate buffer, pH 5.0, at 37.degree.. The enzyme was strongly inactivated by iodoacetic acid, HgCl2, and diisopropyl fluorophosphate at pH 5.0. No inhibition of the enzyme was obsd. in the presence of EDTA or 1,10-phenanthroline. .