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Apon Zaenal Mustopa
LIPI Bioteknologi
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Immunology & microbiology Medicine & Pharmacology

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The Purification Of Rennin-Like Protease From Lactobacillus Paracasei Isolated From Ettawa Goat Milk Wendry Setiyadi Putranto; Apon Zaenal Mustopa; Arizah Kusumawati; Anika Prastyowati
ANNALES BOGORIENSES Vol 24, No 2 (2020): Annales Bogorienses
Publisher : Research Center for Biotechnology - Indonesian Institute of Sciences (LIPI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2020.v24.n2.74-80

Abstract

There is a protease produced by bateria that has characteristics similar to rennin from a calf.  Rennin has the ability to clot casein in milk. Rennin-like protease (RLP) is produced by bacteria extracellularly. Lactic Acid Bacteria (LAB) have the potential to be developed for RLP production because they are safe and non-pathogenic bacteria. Rennin is needed in the process of milk coagulation to subsequently obtain a curd in the process of making cheese. In this study, the LAB isolated from Ettawa goat milk (isolate 2.12) which produced RLP was 99% identical to Lactobacillus paracasei based on 16S rRNA gene sequence analysis. The purification of the RLP L. paracasei 2.12 with 60% ammonium sulfate deposition, dialysis, and filtration gel chromatography Sephadex G-50 showed a single 38 kDa protein band with SMCA/SPA was 4.48 higher than that of the calf rennet with a ratio value of 1, therefore in this study, RLP L. paracasei 2.12  was developed as an alternative to renin in cheese making.
Co-Authors Anika Prastyowati Arizah Kusumawati Wendry Setiyadi Putranto