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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Simkhada, J.R., Cho, S.S., Choi, H.S. et al. A new thermolabile alkaline phospholipase D from Streptomyces sp. CS628. Biotechnol Bioproc E 15, 595–602 (2010). https://doi.org/10.1007/s12257-010-0013-3
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DOI: https://doi.org/10.1007/s12257-010-0013-3