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Updated: Jun 6, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Purification, biochemical characterization, and cloning of phospholipase D from Streptomyces racemochromogenes strain
Yozo Nakazawa1, Yoshimasa Sagane, Teppei Kikuchi
1Department of Food and Cosmetic Science, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri, Hokkaido 099-2493, Japan. y3nakaza@bioindustry.nodai.ac.jp
Abstract:
We previously isolated Streptomyces racemochromogenes strain 10-3, which produces a phospholipase D (PLD) with high transphosphatidylation activity. Here, we purified and cloned the PLD (PLD103) from the strain. PLD103 exerted the highest hydrolytic activity at a slightly alkaline pH, which is in contrast to the majority of known Streptomyces PLDs that have a slightly acidic optimum pH. PLD103 shares only 71-76% amino acid sequence identity with other Streptomyces PLDs that have a slightly acidic optimum pH; thus, the diversity in the primary structure might explain the discrepancy observed in the optimum pH. The purified PLD displayed high transphosphatidylation activity in the presence of glycerol, L: -serine, and 2-aminoethanol hydrochloride with a conversion rate of 82-97% in a simple one-phase system, which was comparable to the rate of other Streptomyces PLDs in a complicated biphasic system.
