Jayanthi, Nalista and Purwanto, Maria Goretti Marianti and Chrisnasari, Ruth and Pantjajani, Tjandra and Wahjudi, A. and Sugiarto, M. (2018) Characterization of thermostable chitinase from Bacillus licheniformis B2. In: The 2nd International Conference on Natural Resources and Life Sciences (NRLS-2018), 23–24 August 2018, Ibis Styles Hotel, Surabaya, Indonesia.
PDF
Maria Goretti_Characterization of thermostable chitinase.pdf Download (2MB) |
Abstract
Chitinases is an enzyme capable of degrading chitin into oligomers to produce chitin derivatives products which are more useful. Thermostable-chitinase is of important in the relevant industrial application, since the degradation process oftently requires prety high temperature. This research report a characterization of chitinase isolated from thermophilic microorganism. The chitinase was obtained from Bacillus licheniformis B2 isolated from Ijen hot spring, East Java. It has the best chitinolytic activity at pH 7 when colloidal chitin was used as substrate. The enzyme exhibited activity in broad temperature range, from 50 °C to 70 °C, optimally at 55 °C. It was stable at 50 °C up to 90 min, at 60 °C up to 60 min and at 70 °C up to 30 min. At neutral pH this enzyme has negative charge but further purification is needed to determine its pI. The Km and Vmax of this chitinase for colloidal chitin were 101.96 mg mL‒1 and 2.72 μmol (min mL)‒1, respectively. Addition of NaCl, KNO3 and MgSO4 decreased the activity of chitinase following mixed inhibitor mode. This enzyme should be a good candidate for applications in the recycling of chitin waste.
Item Type: | Conference or Workshop Item (Paper) |
---|---|
Uncontrolled Keywords: | Bacillus licheniformis, chitinase, shellfish waste, waste to food |
Subjects: | Q Science > Q Science (General) |
Divisions: | Faculty of Technobiology > Department of Biology |
Depositing User: | Ester Sri W. 196039 |
Date Deposited: | 30 Jul 2019 01:55 |
Last Modified: | 22 Nov 2021 04:40 |
URI: | http://repository.ubaya.ac.id/id/eprint/35226 |
Actions (login required)
View Item |