Characterization of partially extracellular proteases from bekasam-isolated Lactobacillus plantarum S31 and its application to hydrolyze skimmed-milk with antibacterial property

Budiarto B. R., . and Mustopa A. Z., . and Idarmawan T., . Characterization of partially extracellular proteases from bekasam-isolated Lactobacillus plantarum S31 and its application to hydrolyze skimmed-milk with antibacterial property. pp. 340-349. ISSN 2231-7546

The extracellular proteases secrected by L. plantarum S31 has been isolated and purified from supernatant of 20-day cultivation when the cells was at the stationary phase. The isolated proteases showed two distinct proteolytic activity named LPS31.18 and LP31.37 on zymogram assay after sequentially purified using 80 ammonium sulphate ammonium sulphate saturation and sephadex G-50 with overall specific activity of 2 IU/mg and purity fold of 8.01. Furthermore the partially purified enzymes exhibited thermostable characteristic and were considerably active at pH 5. The activity of the enzymes enzymes was mostly inhibited in the presence in the presence of PMSF EDTA and Tween-20 meanwhile cofactors (Mg2 and Ca2) SDS and DTT tend tended to increase caseinolytic activity. These enzymes were also usable to generate bioactive peptides from skimmed-milk as proven by bacterial-killing property of skimmed-milk hydrolysate towards food spoilage-causing bacteria such as E. coli and L. monocytogenes.

Full text available from: Official URL: http://www.ifrj.upm.edu.my/23%20(01)%202016/(50).p...

Abstract

The extracellular proteases secrected by L. plantarum S31 has been isolated and purified from supernatant of 20-day cultivation when the cells was at the stationary phase. The isolated proteases showed two distinct proteolytic activity named LPS31.18 and LP31.37 on zymogram assay after sequentially purified using 80 ammonium sulphate ammonium sulphate saturation and sephadex G-50 with overall specific activity of 2 IU/mg and purity fold of 8.01. Furthermore the partially purified enzymes exhibited thermostable characteristic and were considerably active at pH 5. The activity of the enzymes enzymes was mostly inhibited in the presence in the presence of PMSF EDTA and Tween-20 meanwhile cofactors (Mg2 and Ca2) SDS and DTT tend tended to increase caseinolytic activity. These enzymes were also usable to generate bioactive peptides from skimmed-milk as proven by bacterial-killing property of skimmed-milk hydrolysate towards food spoilage-causing bacteria such as E. coli and L. monocytogenes.

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Item Type:	Article
AGROVOC Term:	Lactobacillus plantarum
AGROVOC Term:	Skimmed milk
AGROVOC Term:	Hydrolyzed proteins
AGROVOC Term:	Proteases
AGROVOC Term:	Extracellular fluid
AGROVOC Term:	Lactic acid bacteria
AGROVOC Term:	Antibacterial properties
Depositing User:	Ms. Suzila Mohamad Kasim
Last Modified:	24 Apr 2025 06:27
URI:	http://webagris.upm.edu.my/id/eprint/22498

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