Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis.
نویسندگان
چکیده
Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM(-1) s(-1). Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5 degrees C.
منابع مشابه
New penicillin acylase activity for aculeacin A acylase from Actinoplanes utahensis
Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans 1 revealed new acylase activities being able to hydrolyse penicillin V and several natural 2 aliphatic penicillins. Penicillin K was the best substrate showing a catalytic efficiency of 3 34.79 mM-1 s-1. Furthermore, aculeacin A acylase was highly thermostable with a midpoint 4 transition temperature (Tm) of 81.5º...
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Here, we describe the draft genome sequence of Actinoplanes utahensis NRRL 12052, a filamentous bacterium that encodes an aculeacin A acylase and a putative N-acyl-homoserine lactone acylase of biotechnological interest. Moreover, several nonribosomal peptide synthase (NRPS) and polyketide synthase (PKS) clusters and antibiotic resistance genes have been identified.
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Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...
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ورودعنوان ژورنال:
- Applied and environmental microbiology
دوره 73 16 شماره
صفحات -
تاریخ انتشار 2007