Abstract

A NOVEL ALKALINE INTRACELLULAR PENICILLIN V ACYLASE FROM STREPTOMYCES SP. APT13: IDENTIFICATION AND EFFECT OF PHYSIOCHEMICAL CONDITIONS ON ENZYME PRODUCTION

Philem Pushparani Devi, Tanvi Godbole, Asmita Prabhune*

ABSTRACT

Penicillin V acylase (EC 3.5.1.11) is an industrially important enzyme, used for the production of 6-aminopenicillanic acid (6-APA), a key intermediate in manufacture of semi synthetic β-lactam antibiotics. The enzyme is produced both intracellularly and extracellularly by bacteria, actinomycetes and fungi. So far, very few reports are available on penicillin V acylase from actinomycetes. In the present study, we report isolation of novel intracellular penicillin V acylase producingactinomycetes, Streptomyces sp. APT13 and the effect of media components to gain an insight on the conditions effecting intracellular penicillin V acylase production. Enzyme activity was increased 3 fold in a medium with casein as carbon and nitrogen source. The enzyme production was found constitutive and enhanced by nutrient stress. Optimum activity was shown at pH 9.0, which is the most alkaline reported so far pertaining to intracellular penicillin V acylases. Enzyme activity was optimum at 50 ° C. Magnesium was essential for enzyme production and deletion of calcium from the basal medium increased enzyme production which accompanied mycelial aggregation.

Keywords: Penicillin V acylase, 6-APA, Streptomyces sp. APT13, Casein.