ISSN: 0973-7510

E-ISSN: 2581-690X

Research Article | Open Access
Jendri Mamangkey1, Dwi Suryanto1 , Erman Munir1 and Apon Zaenal Mustopa2
1Department of Biology, Faculty of Mathematics and Natural Sciences, Universitas Sumatera Utara, Medan, 20155, Indonesia.
2Research Centre for Biotechnology, Indonesian Institute of Science (LIPI), Bogor, Indonesia.
J Pure Appl Microbiol. 2020;14(2):1203-1211 | Article Number: 6041 | © The Author(s). 2020
Received: 13/01/2020 | Accepted: 26/05/2020 | Published: 22/06/2020

Keratinase is a proteolytic enzyme capable on degrading the hardy polymeric biomolecule or keratin. In recent days, the utilization of keratinolytic microorganisms is seen as a promising way in recycling the keratin wastes from the avian and mammalians into valuable derived products. Previous study has reported the presence of a keratinolytic bacterium, later identified as Azotobacter chroococcum B4 obtained from dump soils. The present study investigates the enzyme characteristics of keratinase produced by this strain based on the physical appearance of final degraded product using SEM, the molecular weight of keratinase using SDS-PAGE, the effects of nutrition (C/N-source) on strain production of keratinase and the enzyme stability in metal ions solution. The molecular weight of keratinase produced by A. chroococcum B4 was about 30 kDa. Both sucrose and tryptone supplementation increase the keratinase activity by 71.7 and 97.8 U/mL after 96 h of cultivation. Metal ions, Ca2+, Mg2+, Mn2+, Na+, and K+ are regarded as activators by increasing the relative activity of keratinase by 117, 166, 111, 113, and 112% respectively, while phenylmethylsulfonyl flouride (PMSF) is regarded as inhibitor by decreasing the relative activity down to 31%. Based on the metal ion characteristics, this strain produced a serine-protease type of keratinase which may further studied for its application in the field.


Azotobacter chrocoocum, keratinase, sucrose, tryptone

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