Partial Purification and Some Properties of a Phospholipase C fromPseudomonassp. Strain KS3.2 | Zendy

Daisuke Sugimori | Zendy; Masatoshi Nakamura | Zendy

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Partial Purification and Some Properties of a Phospholipase C fromPseudomonassp. Strain KS3.2

Author(s) -

Daisuke Sugimori,

Masatoshi Nakamura

Publication year - 2006

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.70.535

Subject(s) - enzyme , strain (injury) , pseudomonas , phospholipase c , enzyme assay , phosphatidylcholine , chemistry , biochemistry , peptide , phospholipase , extracellular , chromatography , biology , bacteria , phospholipid , membrane , anatomy , genetics

An extracellular phospholipase C was partially purified from Pseudomonas sp. strain KS3.2. The enzyme was composed of an approximately 18-kDa peptide. Maximal enzyme activity was found at pH 7.2 and 50 degrees C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 degrees C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activity toward other phospholipids.

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