Production, purification and characterization of the α-amylase from local bacteria isolate Bacillus subtilis ITBCCB148

Yandri,; Witazora, Y; Suhartati, Tati; Satria, Heri; Hadi, Sutopo

doi:10.1088/1742-6596/1751/1/012096

Cited by 6 publications

(6 citation statements)

References 7 publications

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“…The study procedures were based on a previous study, comprising production, isolation, partial purification, immobilization, and characterization of the soluble and immobilized enzymes [ 12 ]. Furthermore, the crude enzyme was soluble by fractionation using ammonium sulphate and dialysis as described in [ 13 ], while the immobilization method was based on [ 10 ].…”

Section: Methodsmentioning

confidence: 99%

The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

Yandri

Tiarsa

Suhartati

et al. 2022

Biochemistry Research International

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The stability of the α-amylase enzyme has been improved from Aspergillus fumigatus using the immobilization method on a bentonite matrix. Therefore, this study aims to obtain the higher stability of α-amylase enzyme from A. fumigatus; 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 (KM), maximum velocity V max , thermal inactivation rate constant (ki), half-life (t1/2), and the change of energy due to denaturation (ΔGi). The results showed that the soluble enzyme has an optimum temperature of 55°C, KM of 3.04 mg mL−1 substrate, V max of 10.90 μmole mL−1 min−1, ki of 0.0171 min−1, t1/2 of 40.53 min, and ΔGi of 104.47 kJ mole−1, while the immobilized enzyme has an optimum temperature of 70°C, KM of 8.31 mg mL−1 substrate, V max of 1.44 μmole mL−1 min−1, ki of 0.0060 min−1, t1/2 of 115.50 min, and ΔGi of 107.37 kJ mole−1. Considering the results, the immobilized enzyme retained 42% of its residual activity after six reuse cycles. Additionally, the stability improvement of the α-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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Section: Methodsmentioning

confidence: 99%

The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

Yandri

Tiarsa

Suhartati

et al. 2022

Biochemistry Research International

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“…Amylase was produced in fermentation media containing starch (0.5%), yeast extract (0.5%), KH 2 PO 4 (0.05%), MgSO 4 .7H 2 O (0.02%), and CaCl 2 .2H 2 O (0.01%) with a pH of 6.5. Fermentation temperature was 32°C with 72 h fermentation time [17,18].…”

Section: Production Of -Amylasementioning

confidence: 99%

“…-amylase produced was isolated from the fermentation medium using a cold centrifuge at 5000 rpm for 20 min to obtain a crude extract of the enzyme [17].…”

Section: Isolation Of -Amylasementioning

confidence: 99%

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

Yandri¹,

Suhartati²,

Satria³

et al. 2021

J Adv Pharm Educ Res

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“…Sebanyak 2% media inokulum dari jumlah media fermentasi dimasukkan ke dalam media fermentasi secara aseptis lalu dikocok dalam shaker incubator dengan kecepatan 1500 rpm pada 29 °C (Yandri et al, 2010). Enzim α-amilase diisolasi dengan cara memisahkan antara filtrat dan endapan, menggunakan sentrifugasi dengan kecepatan 5000 rpm selama 15 menit.…”

Section: Prosedur Produksi Dan Isolasi Enzimunclassified

Peningkatan Kestabilan Enzim Α–amilase Dengan Penambahan Gliserol

Yandri¹,

Nadila²,

Suhartati³

et al. 2020

Anal.Environ.Chem

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Enzim α-amilase adalah enzim yang mengkatalisis hidrolisis ikatan α-1,4 glikosidik polisakarida menghasilkan dekstrin, oligosakarida, maltosa, dan Dglukosa. Penelitian ini bertujuan meningkatkan kestabilan enzim α-amilase hasil pemurnian dari Aspergillus fumigatus dengan penambahan gliserol. Aktivitas enzim ditentukan dengan metode Fuwa dan Mandels, sedangkan kadar protein ditentukan dengan metode Lowry. Hasil penelitian menunjukkan enzim hasil pemurnian memiliki aktivitas spesifik sebesar 1,377 U/mg meningkat sebanyak 8,1 kali dibandingkan dengan ekstrak kasar enzim yang memiliki aktivitas spesifik sebesar 0,170 U/mg. Enzim hasil pemurnian memiliki pH optimum 5,5; suhu optimum 55 °C; waktu paruh 133,26 menit. Enzim setelah penambahan gliserol 0,5; 1 dan 1,5 M memiliki pH optimum dan suhu optimum yang sama, yaitu pH 5,5 dan suhu 55 °C. Enzim setelah penambahan gliserol: 0,5 M memiliki waktu paruh 157,5 menit: 1 M memiliki waktu paruh 182,36 menit, dan 1,5 M memiliki waktu paruh 223,54 menit. Penambahan gliserol pada enzim α-amilase hasil pemurnian dari A. fumigatus dapat meningkatkan kestabilan enzim sebanyak 1,2-1,7 kali dibandingkan dengan enzim hasil pemurnian yang ditunjukkan dengan peningkatan waktu paruh.

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Production, purification and characterization of the α-amylase from local bacteria isolate Bacillus subtilis ITBCCB148

Cited by 6 publications

References 7 publications

The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

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

Peningkatan Kestabilan Enzim Α–amilase Dengan Penambahan Gliserol

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