| Literature DB >> 31388216 |
Sanjay K S Patel1, Rahul K Gupta1, Virendra Kumar1, Primata Mardina1, Rowina Lestari1, Vipin C Kalia1, Myung-Seok Choi1, Jung-Kul Lee1.
Abstract
Immobilization of enzymes through metal-based system is demonstrated as a promising approach to enhance its properties. In this study, the influence of metals ions, including copper, cobalt and zinc (Zn) on the immobilization of β-glucosidase (BGL) through the synthesis of protein-inorganic hybrid was evaluated at 4 °C. Among these metal ions-based hybrids, Zn showed the highest encapsulation yield and relative activity of 87.5 and 207%, respectively. Immobilized BGL exhibited higher pH and temperature stability compared to free form. Thermal stability of hybrid improved up to 26-fold at 60 °C. After 10 cycles of reuse, immobilized enzyme retained 93.8% of residual activity. These results suggested that metal ions played a significant role in the enzyme immobilization as a protein-inorganic hybrid. Overall, this strategy can be potentially applied to enhance the properties of enzymes though effective encapsulation for the broad biotechnological applications.Entities:
Keywords: Immobilization; Protein-inorganic hybrid; Reusability; Stability; β-Glucosidase
Year: 2019 PMID: 31388216 PMCID: PMC6646435 DOI: 10.1007/s12088-019-00796-z
Source DB: PubMed Journal: Indian J Microbiol ISSN: 0046-8991 Impact factor: 2.461