Development and characterization of cross-linked enzyme aggregates of thermotolerant alkaline protease from Bacillus licheniformis.

Autor: Bashir F; Department of Biochemistry, Faisalabad, Pakistan., Asgher M; Department of Biochemistry, Faisalabad, Pakistan. Electronic address: masgher63@uaf.edu.pk., Hussain F; Department of Biochemistry, Faisalabad, Pakistan., Randhawa MA; National Institute of Food Science and Technology, University of Agriculture Faisalabad, Faisalabad, Pakistan.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2018 Jul 01; Vol. 113, pp. 944-951. Date of Electronic Publication: 2018 Mar 03.
DOI: 10.1016/j.ijbiomac.2018.03.009
Abstrakt: An alkaline protease was produced by B. licheniformis with 132.43±3.4U/mL activity in LSF which was further enhanced by optimizing culture conditions. The optimum enzyme activity (148.9±4.1U/mL) was harvested at pH7.5; temperature, 40°C and inoculum, 1.5mL after 48h incubation. Alkaline protease was immobilization by forming cross linked enzyme aggregates (CLEAs) and the processes of CLEAs formation was also optimized. The protease CLEAs developed using 80% ammonium sulfate, 65mM glutaraldehyde and 0.11mM BSA showed best activity recovery (39.76%). Free protease and CLEAs were characterized and compared. It was observed that CLEAs of protease exhibited broad pH range with best activity at pH10. The immobilized protease was also thermo-tolerant with optimum activity at 65°C temperature. The V max and K m of protease-CLEAs were 125.5U/mL and 18.97μM, respectively as compared to 104.9U/mL and 29μM, respectively for free protease. It was concluded that immobilized enzyme in the form of CLEAs is a valuable catalyst for potential industrial applications.
(Copyright © 2018 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: