期刊
BIOCATALYSIS AND AGRICULTURAL BIOTECHNOLOGY
卷 29, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bcab.2020.101818
关键词
Lactobacillus; Rennin like protease; Milk clotting activity; Characterization
Cheese processing requires rennin during curdling process. A rennin like protease was extracted from Lactoba-cillus plantarum 1.13 isolated from Bakasam (traditional fermented meat) and characterized. The novel rennin like protease was purified by ammonium sulphate precipitation and gel filtration (Sephadex G-50) chromatography. The extracellular enzyme showed spesific Milk Clotting Activity (MCA) of 414.67 SU/mg after purification. The ratio of SMCA/SPA is 5.46 higher than Mucor pusillus QM 436 with value 1.81. Biochemical characterization indicated that optimum rennin like protease were at pH 4 at 40 degrees C. This enzyme was activated by 10 mM CaCl2 and 5 mM MgCl2, but inhibited by 5 mM EDTA and 0.5 mM PMSF. The SDS-PAGE and zymogram analysis indicated a 24.3 kDa enzyme with MCA/PA showed potential to be used as alternative of rennin in cheese making.
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