A new thermolabile alkaline phospholipase D from <Emphasis Type="Italic">Streptomyces</Emphasis> sp. CS628 |
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Authors: | Jaya Ram Simkhada Seung Sik Cho Hong Seok Choi Si Wouk Kim Hei Chan Lee Jae Kyung Sohng Jin Cheol Yoo |
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Institution: | 1.Department of Pharmacy, College of Pharmacy,Chosun University,Gwangju,Korea;2.Department of Environmental Engineering, BK 21 Team for Biohydrogen Production,Chosun University,Gwangju,Korea;3.Institute of Biomolecule Reconstruction,Sun Moon University,Asan,Korea |
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Abstract: | 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°C 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°C, pH 5.7
∼ 10.6 and ≤30°C, 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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