Repo Dosen ULM

Influence of Metal Ions on the Immobilization of β-Glucosidase Through Protein-Inorganic Hybrids

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dc.contributor.author Patel, Sanjay K. S.
dc.contributor.author Gupta, Rahul K.
dc.contributor.author Kumar, Virendra
dc.contributor.author Mardina, Primata
dc.contributor.author Lestari, Rowina
dc.contributor.author Kalia, Vipin C.
dc.contributor.author Choi, Myung-Seok
dc.contributor.author Lee, Jung-Kul
dc.date.accessioned 2022-07-28T01:03:43Z
dc.date.available 2022-07-28T01:03:43Z
dc.date.issued 2019-03
dc.identifier.issn 0973-7715
dc.identifier.uri https://repo-dosen.ulm.ac.id//handle/123456789/24912
dc.description.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 immobi lization of b-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 sta bility 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 biotechno logical applications en_US
dc.language.iso en en_US
dc.publisher Springer en_US
dc.subject b-Glucosidase en_US
dc.subject Immobilization en_US
dc.subject Protein-inorganic hybrid en_US
dc.subject Reusability en_US
dc.subject Stability en_US
dc.title Influence of Metal Ions on the Immobilization of β-Glucosidase Through Protein-Inorganic Hybrids en_US
dc.type Article en_US


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