Physiologie und Biochemie der Streptomyceten VIII. Esteraseaktivität und Turimycin-Bildung in Kulturen von Streptomyces hygroscopicus JA 6599

✍ Scribed by Prof. Dr. G. Reuter; B. Hüttner

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 454 KB
• Volume: 17
• Category: Article
• ISSN: 0233-111X
• DOI: 10.1002/jobm.19770170107

✦ Synopsis

Abstract

Esterase in cell‐free extracts of Streptomyces hygroscopicus JA 6599 has a temperature‐optimum of 35 °C, a pH‐optimum with p‐nitrophenylacetate as substrate at pH 7.7–8.1, with α‐naphthylacetate at pH 7–9. MICHAELIS constants in cell‐free extracts: with α‐naphthylacetate K~m~ = = 0.71 mM, with p‐nitrophenylacetate K~m~ = 0.21 mM. Phenylesters were better hydrolyzed than naphthylesters, phenylacetate was best hydrolyzed; β‐naphthylacetate was better hydrolyzed than α‐naphthylacetate. Among the naphthylesters the ester of propionic acid was hydrolyzed best. Caprylate, stearate, and 0,0‐diethyl‐0‐(‐p‐nitrophenyl)‐phosphate inhibit the splitting of α‐naphthylacetate. A comparison with esterases of other biological origin shows that the enzyme studied can be a carboxylesterase (E.C. 3.1.1.1.). In cultures of JA 6599 V~13~ and JA 6599‐6 the change of esterase activity during the fermentation was determined. We found a correlation between the enzymatic activity and the antibiotic‐concentration in the culture medium.