OPTIMASI PRODUKSI KITINASE DAN IDENTIFIKASI MOLEKULER BAKTERI KITINOLITIK BK-1 DARI CAIRAN Nepenthes mirabilis (Lour) Druce ASAL HPPB UNIVERSITAS ANDALAS

Hania, Titami (2024) OPTIMASI PRODUKSI KITINASE DAN IDENTIFIKASI MOLEKULER BAKTERI KITINOLITIK BK-1 DARI CAIRAN Nepenthes mirabilis (Lour) Druce ASAL HPPB UNIVERSITAS ANDALAS. Masters thesis, Universitas Andalas.

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Abstract

Chitinase is an enzyme that can catalyze the degradation reaction (breakdown) of β-(1,4) glycosidic chitin compounds and produce oligosaccharides or N�Acetylglucosamine monomers. Chitin-derived products, such as glucosamine and N-Acetylglucosamine, have high economic value as alternative raw materials in various industries such as food, cosmetics, pharmaceutical and other chemical industries. Chitinase is produced by chitinolytic microorganisms that are mostly found in the soil and water environment. This study aims to determine the optimization of pH (7, 8 and 9), substrate type (colloidal chitin, chitin and chitosan), and substrate concentration (1%, 2%, 3%, 4% and 5%) on chitinase activity of BK�1 isolate. As well as knowing the characterization and molecular identification of chitinolytic bacterial isolate BK-1. The research method was conducted in a survey with the stages of pH optimization, type of substrate, substrate concentration, and characterization and molecular identification of isolate BK-1. The results showed that the optimum condition in producing chitinase enzyme in isolate BK-1 was with medium pH 7, colloidal chitin substrate type, and 2% substrate concentration. The optimum condition of chitinase production from isolate BK-1 Nepenthes mirabilis in colloidal chitin medium pH 7 on day 2 chitinase activity value of 0.1428, then chitinase activity in the treatment of colloidal chitin substrate type obtained 0.2203 U/mL on day 2 and in the treatment of 2% substrate concentration obtained an activity value of 0.2203 U/mL on day 2, while the character of isolate BK-1 is Bacil cell shape, Gram (+), Catalase (+), Endospores sub terminal and motile. And molecular-based analysis of isolate BK-1 has similarities with Bacillus cereus strain CUMB NS 07.

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