Stability enhancement of Bacillus subtilis ITBCCB148 originating -amylase by immobilization using chitin

Yandri, Yandri; Suhartati, Tati; Satria, Heri; Karlinasari, Surtini; Yuwono, Suripto Dwi; Hadi, Sutopo

doi:10.51847/fzqcrn5wmd

Cited by 3 publications

(2 citation statements)

References 23 publications

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“…In the immobilization process via physical adsorption, the enzyme only can be bound onto supporting matrix at certain pH. The enzyme anionic form exists due to deprotonation of the amine group, while the OH groups in water molecules make the hybrid surface charge positive at higher solution pH [ 27 , 32 ]. Since oppositely charged groups are due to the electrostatic interaction, the enzyme can be adsorbed to the positively charged active sites of the hybrid surface by the cation-exchange process [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid

Tiarsa

Yandri

Suhartati

et al. 2022

Biochemistry Research International

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Enzyme immobilization is a powerful method to improve the stability, reuse, and enzymatic properties of enzymes. The immobilization of the α-amylase enzyme from Aspergillus fumigatus on a chitin-bentonite (CB) hybrid has been studied to improve its stability. Therefore, this study aims to obtain the higher stability of α-amylase enzyme to reduce industrial costs. The procedures were performed as follows: production, isolation, partial purification, immobilization, and characterization of the free and immobilized enzymes. The CB hybrid was synthesized by bentonite, chitin, and glutaraldehyde as a cross-linker. The free enzyme was immobilized onto CB hybrid using 0.1 M phosphate buffer pH 7.5. The free and immobilized enzymes were characterized by optimum temperature, Michaelis constant (KM), maximum velocity V max , thermal inactivation rate constant (ki), half-life (t1/2), and transformation of free energy because of denaturation (ΔGi). The free enzyme has optimum temperature of 55°C, KM = 3.04 mg mL−1 substrate, V max = 10.90 μ molemL − 1 min − 1 , ki = 0.0171 min−1, t1/2 = 40.53 min, and ΔGi = 104.47 kJ mole−1. Meanwhile, the immobilized enzyme has optimum temperature of 60°C, KM = 11.57 mg mL−1 substrate, V max = 3.37 μ molemL − 1 min − 1 , ki = 0.0045 min−1, t1/2 = 154.00 min, and ΔGi = 108.17 kJ mole−1. After sixth cycle of reuse, the residual activity of the immobilized enzyme was 38%. The improvement in the stability of α-amylase immobilized on the CB hybrid based on the increase in half-life was four times of the free enzyme.

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Section: Resultsmentioning

confidence: 99%

The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid

Tiarsa

Yandri

Suhartati

et al. 2022

Biochemistry Research International

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“…The enzymes bound to the chitin matrix also have greater thermal activity than that of free enzymes. Table 4 130–150 displays examples of recent research that used chitin-based supports to enhance the stability and activity of enzymes.…”

Section: Chitin-based Supports (Carriers) For Enzyme Immobilizationmentioning

confidence: 99%

Biomass-derived functional materials as carriers for enzymes: towards sustainable and robust biocatalysts

et al. 2023

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Challenges and prospects of microbial α-amylases for industrial application: a review

Ashok,

Dasgupta,

Ray

et al. 2023

World J Microbiol Biotechnol

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Stability enhancement of Bacillus subtilis ITBCCB148 originating -amylase by immobilization using chitin

Cited by 3 publications

References 23 publications

The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid

The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid

Biomass-derived functional materials as carriers for enzymes: towards sustainable and robust biocatalysts

Challenges and prospects of microbial α-amylases for industrial application: a review

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