Ilmi Syifaul Maula, Andriyani Andriyani, Abdul Hadjranul Fatah, Suharti Suharti
Keratin is a protein that is very difficult to break down. One of the ways to degrade keratin is enzymatic degradation using keratinase. Keratinase plays an important role in the leather tanning industry, so it is necessary to explore keratinase-producing microbes. This study used isolate GAM15 from the peat soil of Palangka Raya, Central Kalimantan. The research stages were rejuvenation of protease-producing microbes, determination of isolate purity and identification of phenotypic morphology of isolates, a test of ability to degrade chicken feathers, determination of keratinase character, optimization of keratinase production using chicken feather substrate, and genotypic identification. The optimum GAM15 keratinase at pH 6, temperature 43°C, and the addition of Mg2+and Ca2+ions had no effect on keratinase activity. Optimal keratinase production was optimized on the second day and media at pH 5 with an activity value of 7,829 U/mL. In determining the moisture ratio, the keratinase activity was 9.079 U/mL with a mass of chicken feather substrate and a volume of saline solution at a humidity of 1:3. The percent weight loss after optimization is 12.9%. GAM15 isolate is a type of microbe that already exists and has a similarity percentage of 100.00% to the Bacillus proteolytic strain MCCC 1A00365 species. © 2023 American Institute of Physics Inc.. All rights reserved.
Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, Jl Semarang No. 5, Malang, 65145, Indonesia; Department of Chemistry, FKIP, University of Palangka Raya, Palangka Raya, Indonesia
