Purification and properties of a novel glycine amino peptidase from Actinomucor elegans and its potential application.
OBJECTIVE
To study the properties and show the potential application of a glycine aminopeptidase from Actinomucor elegans.


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 degrees C and at pH 8.0 it showed its highest activity. The Km and Kcat of the enzyme for glycine-beta-naphthylamine was 0.24 mm and 100.8 s(-1), respectively. Zinc, copper, cadmium and o-phenanthrolin suppressed almost all enzyme activities at the concentration of 1.0 mm. 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.


CONCLUSIONS
This study demonstrates the properties of a novel aminopeptidase and shows its potential application in the process of the food industry.
Ma
X
X
Institute of Microbiology, College of Life Sciences, Zhejiang University, Hangzhou, China. maxiaohong@zju.edu.cn
Zhou
X
X
Yoshimoto
T
T
D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D004355:Drug Stability; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005285:Fermentation; D005658:Fungi / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007218:Industrial Microbiology; D008970:Molecular Weight; D045730:Soy Foods; D013379:Substrate Specificity; D013696:Temperature
D004791:Enzyme Inhibitors; D000626:Aminopeptidases; C020824:glycyl aminopeptidase; D005998:Glycine