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KMID : 0903519930360060539
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1993 Volume.36 No. 6 p.539 ~ p.546
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Purification and partial characteristics of intracellular aminopeptidase from Micrococcus sp . LL3
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Abstract
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This paper describes the purification and partial characteristics of aminopeptidase from Microccus sp. LL3 to utilize the microorganism as a potential agent for industrial application for the purpose of shortening ripening period of cheddar cheese. The optimal temperature and pH for enzyme activity were 35℃ and 7.0, respectively for L-leucine -p-nitroanilide as substrate. The enzyme remained stable for 10 minutes up to 50℃. The activity of aminopeptidase was stimulated by Mg^(++) ion but strongly inhibited by Hg^(++), metal complexing reagents, ethylenediaminetetraacetate (EDTA) and 1,10-phenanthroline. The enzyme was thought to be metallopeptidase. This enzyme had a broad substrate specificity, but was inactive on peptide with arginine as N-terminal amino acid. An intracellular aminopeptidase from Micrococcus sp. LL3 was purified by chromatography on DEAE-Sephacel and filtration on Sepacryl S-300. The enzyme has a molecular weight of 43,500.
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