Journal
BIOTECHNOLOGY LETTERS
Volume 31, Issue 3, Pages 429-435Publisher
SPRINGER
DOI: 10.1007/s10529-008-9890-3
Keywords
Alkalo- and thermostable; One-step purification; Phospholipase D; Streptomyces olivochromogenes
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Funding
- Ministry of Commerce, Industry, and Energy ( MOCIE), Republic of Korea [RT104-03-03]
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A 60 kDa phospholipase D (PLD) was obtained from Streptomyces olivochromogenes by one-step chromatography on Sepharose CL-6B. Maximal activity was at pH 8 and 75A degrees C and the enzyme was stable from pH 7 to 13 and from 55 to 75A degrees C. Thermal and pH stability with temperature optimum of the enzyme were highest among Streptomyces PLDs reported so far. The activity was Ca2+-dependent and enhanced by detergents. The Km and Vmax values for phosphatidylcholine were 0.6 mM and 650 mu mol min(-1) mg(-1), respectively. In addition, the enzyme also revealed transphosphatidylation activity, which was optimum at pH 8 and 50A degrees C. The first 15 amino acid residues of the N terminal sequence were ADYTPGAPGIGDPYY, which are significantly different from the other known PLDs. The enzyme may therefore be a novel PLD with potential application in the lipid industry.
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