Purification,Biochemical Characterization,and Cloning of Phospholipase D from <Emphasis Type="Italic">Streptomyces racemochromogenes</Emphasis> Strain 10-3 |
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| Authors: | Yozo Nakazawa Yoshimasa Sagane Teppei Kikuchi Masataka Uchino Takeshi Nagai Hiroaki Sato Kazuki Toeda Katsumi Takano |
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| Institution: | 1.Department of Food and Cosmetic Science, Faculty of Bioindustry,Tokyo University of Agriculture,Hokkaido,Japan;2.Sars International Centre for Marine Molecular Biology,Bergen,Norway;3.Department of Applied Biology and Chemistry, Faculty of Applied Bioscience,Tokyo University of Agriculture,Tokyo,Japan |
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| 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. |
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