Open AccessKarakterisasi Protease Ekstraseluler Clostridium spp. T11-3
Author(s) -
Loli Natalia,
Lily Nathalia,
Anja Meryandini
Publication year - 2019
Publication title -
biota
Language(s) - English
Resource type - Journals
eISSN - 2527-323X
pISSN - 2527-3221
DOI - 10.24002/biota.v11i1.2822
Subject(s) - protease , divalent , clostridium , casein , chemistry , enzyme , food science , microbiology and biotechnology , 16s ribosomal rna , biochemistry , proteases , biology , bacteria , organic chemistry , gene , genetics
Protease is one of the leather commercial enzymes which is widely used such in food processing, medicine and leather industry. Clostridium sp T11-3 was isolated from Tiu Jeruk River in Nusa Tenggara Barat. Sequence analysis of 16S rRNA indicated that Clostridium spp T11-3 was closely related to C. bifermentans. This isolate produced maximum protease activity after 18 hours of cultivation in liquid media. Protease of Clostridium spp 11-3 displayed maximum activity at pH 5 and 60oC with casein as substrate. In the presence of 1 mM divalent ion Mg2+ the enzym activity increased to 141 %, while others ion divalent (Ca2+, Zn2+, Cu2+, Fe2+, and Co2+) inhibited protease activity.