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

Academic Article
Publication Date:
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.
Iris type:
01.01 Articolo in rivista
Keywords:
TRANSPHOSPHATIDYLATION; phospholipase D; protein purification
List of contributors:
Carrea, Giacomo; Secundo, Francesco
Authors of the University:
SECUNDO FRANCESCO
Handle:
https://iris.cnr.it/handle/20.500.14243/116712
Published in:
BIOTECHNOLOGY LETTERS
Journal
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