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. Th...
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.