An enzyme with phospholipase D activity was purified to homogeneity from a new strain of Streptomyces. The molecular mass, assessed by electrospray mass spectrometry, was 52672 Da and the isoelectric point 9.2. The enzyme, which had pH optimum between 4 and 7, showed satisfactory stability and transphosphatidylation activity.

Purification and applications of a phospholipase D from a new strain of Streptomyces

Carrea G;Secundo F;
1997

Abstract

An enzyme with phospholipase D activity was purified to homogeneity from a new strain of Streptomyces. The molecular mass, assessed by electrospray mass spectrometry, was 52672 Da and the isoelectric point 9.2. The enzyme, which had pH optimum between 4 and 7, showed satisfactory stability and transphosphatidylation activity.
1997
TRANSPHOSPHATIDYLATION
phospholipase D
protein purification
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/116712
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