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Purification and properties of a novel glycine amino peptidase from Actinomucor elegans and its potential application
Author(s) -
Ma X.,
Zhou X.,
Yoshimoto T.
Publication year - 2004
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1111/j.1365-2672.2004.02373.x
Subject(s) - random hexamer , aminopeptidase , glycine , enzyme , molecular mass , protease , biochemistry , amino acid , chemistry , hydrolysis , zinc , size exclusion chromatography , substrate (aquarium) , protein subunit , enzyme assay , exopeptidase , biology , organic chemistry , leucine , ecology , gene
Aims: To study the properties and show the potential application of a glycine aminopeptidase from Actinomucor elegans . Methods and Results: The enzyme was estimated to have molecular mass of 320 kDa by gel filtration and the subunit size of 56·5 kDa by SDS‐PAGE. It hydrolysed glycine from substrate more efficiently than other amino acids. The optimal temperature for this enzyme was 40°C and at pH 8·0 it showed its highest activity. The K m and K cat of the enzyme for glycine‐ β ‐naphthylamine was 0·24 m m and 100·8 s −1 , respectively. Zinc, copper, cadmium and o ‐phenanthrolin suppressed almost all enzyme activities at the concentration of 1·0 m m . In the process of hydrolysing proteins, it could improve the protease activity considerably. Conclusions: It was a hexamer metalloenzyme which was specific for the substrates with glycinse residue at the N‐terminal and some metal cations were needed to maintain its activity. Significance and Impact of the Study: This study demonstrates the properties of a novel aminopeptidase and shows its potential application in the process of the food industry.