KMID : 1094720100150040595
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Biotechnology and Bioprocess Engineering 2010 Volume.15 No. 4 p.595 ~ p.602
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A new thermolabile alkaline phospholipase D from Streptomyces sp. CS628
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Simkhada Jaya Ram
Cho Seung-Sik Choi Hong-Seok Kim Si-Wouk Lee Hei-Chan Sohng Jae-Kyung Yoo Jin-Cheol
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Abstract
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A phospholipase D (PLD628), constitutively secreted by Streptomyces sp. CS628, was purified by ion exchange with CM Trisacryl and gel filtration with Sepharose CL-6B. The enzyme production was highest with peptone and starch as nitrogen and carbon sources, and at 30¡ÆC with an initial medium pH of 7.5. Molecular weight, optimum pH, optimum temperature, pH stability, and thermostability of the enzyme were 50 kDa, pH 9.6, 30¡ÆC, pH 5.7 ¡ 10.6 and ¡Â30¡ÆC, respectively. Detergents and metal ions had varied effects on the enzyme activity. Importantly, PLD628 could not catalyze transphosphatidylation of glycerol, L-serine, myo-inositol or ethanolamine, which are extensively used to assess the activity, suggesting that PLD628 lacks the transphosphatidylation activity. PLD628 could be a novel PLD based on its biochemical characteristics, which are significantly different from previously reported PLDs, such as thermolability, highest activity at alkaline pH, and lack of transphosphatidylation activity.
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KEYWORD
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thermolabile alkaline phospholipase D, Streptomyces sp. CS628
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