Journal ID : AMA-16-02-2022-11138
[This article belongs to Volume - 53, Issue - 02]
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Abstract :

Proteases are one of most important and abundant enzymes produced by the biotechnology industry, for scientific, physiological and industrial application and dominates the whole enzyme market. Lactobacillus plantarum IIA-1A5 is an Indonesian lactic acid bacteria (LAB) isolated from beef Crossbreed of Ongole cattle. Preliminary analysis on its whole genome sequence indicated that this strain harbours some genes involved in protein degradation and might be promising to be further applied. This study aimed to study the proteolityc characteristic of the crude recombinant protease Lon-Like IIA-1A5. The result showed that crude Lon-like-IIA-1A5 was successfully expressed in a host cell induced with 1 mM IPTG at 37ºC. IPTG induction in culture was carried out at the 3rd hour of incubation with an OD600 of 0.67. Afterwards E. coli started to produce protein which was indicated by a decrease in the growth of e coli until the 5th hour after induction or until the cells were harvested compared to cultures without induction. The Proteolytic characteristic of crude recombinant Lon-Like IIA-1A5 protease was optimal at pH 9 and a temperature of 60 oC. Crude Lon-Like IIA-1A5 recombinant protease activity was increased in toluene, N-hexane, and chloroform solvents and inhibited in acetonitrile and methanol solvents as well as Cu2+, and Zn2+ ions. Crude recombinant Lon-Like IIA-1A5 protease degraded both myofibril protein and gelatin was statistically higher (P<0.05) than casein protein, skim milk, collagen and sarcoplasmic protein, while the ability of this protein to degrade casein protein, skim milk and bovine serum albumin was not different (P>0.05).

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