The Stability Improvement of -Amylase Enzyme from by Immobilization on a Bentonite Matrix.

Biochem Res Int

Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Jl. Prof. Dr. Sumantri Brojonegoro No. 1, Bandar Lampung 35145, Indonesia.

Published: January 2022

The stability of the -amylase enzyme has been improved from using the immobilization method on a bentonite matrix. Therefore, this study aims to obtain the higher stability of -amylase enzyme from ; hence, it is used repeatedly to reduce industrial costs. The procedures involved enzyme production, isolation, partial purification, immobilization, and characterization. Furthermore, the soluble enzyme was immobilized using 0.1 M phosphate buffer of pH 7.5 on a bentonite matrix, after which it was characterized with the following parameters such as optimum temperature, Michaelis constant ( ), maximum velocity ( ), thermal inactivation rate constant ( ), half-life ( ), and the change of energy due to denaturation (Δ ). The results showed that the soluble enzyme has an optimum temperature of 55°C, of 3.04 mg mL substrate, of 10.90 mole mL min, of 0.0171 min, t of 40.53 min, and Δ of 104.47 kJ mole, while the immobilized enzyme has an optimum temperature of 70°C, of 8.31 mg mL substrate, of 1.44 mole mL min, of 0.0060 min, of 115.50 min, and Δ of 107.37 kJ mole. Considering the results, the immobilized enzyme retained 42% of its residual activity after six reuse cycles. Additionally, the stability improvement of the -amylase enzyme by immobilization on a bentonite matrix, based on the increase in half-life, was three times greater than the soluble enzyme.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8763562PMC
http://dx.doi.org/10.1155/2022/3797629DOI Listing

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