通过在膨润土/壳聚糖上吸附固定曲霉α-淀粉酶以增强其稳定性

Emerging Science Journal Pub Date : 2023-10-01 DOI:10.28991/esj-2023-07-05-023

Y. Yandri, Hendri Ropingi, T. Suhartati, Bambang Irawan, S. Hadi

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引用次数: 0

摘要

本研究尝试增强α-淀粉酶的稳定性，结果表明，利用吸附法将α-淀粉酶固定在膨润土/壳聚糖混合基质上，可显著提高从烟曲霉中分离出的α-淀粉酶的稳定性。离心分离出α-淀粉酶，然后用（NH4）2SO4 盐沉淀和透析法精制α-淀粉酶。与粗提取物相比，α-淀粉酶的纯度提高了 19.40 倍。游离α-淀粉酶的最佳温度为 50˚C，而α-淀粉酶/膨润土/壳聚糖的最佳温度为 60˚C。α-淀粉酶/膨润土/壳聚糖的 KM 值为 1.69 ± 0.08 mg mL-1 底物，Vmax 值为 52.32 ± 3.29 µmol mL-1 min-1，而游离α-淀粉酶的 KM 值为 2.56 ± 0.09 mg mL-1 底物，Vmax 值为 3.78 ± 0.09 µmol mL-1 min-1。游离α-淀粉酶的ΔGi值为102.68 ± 0.30 kJ mol-1，t½为21.23 ± 0.23 min，而α-淀粉酶/膨润土/壳聚糖的ΔGi值为104.43 ± 0.00 kJ mol-1，t½为94.29 ± 0.91 min。较高的ΔGi 和 t½ 值表明，α-淀粉酶/膨润土/壳聚糖比游离的α-淀粉酶具有更好的稳定性。另一个重要发现是，α-淀粉酶/膨润土/壳聚糖经过六次循环后，其活性保持率高达 47.61 ± 0.53%，这表明该酶具有在工业中应用的潜力。Doi: 10.28991/ESJ-2023-07-05-023 全文：PDF

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Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement

Stability enhancement attempted in this study demonstrated that significant improvement in the stability of the α-amylase isolated from Aspergillus fumigatus was achieved by immobilizing the enzyme on a bentonite/chitosan hybrid matrix using the adsorption method. Centrifugation was used to isolate the α-amylase, which was then refined using (NH4)2SO4 salt precipitation and dialysis. The purity of the α-amylase improved 19.40 times when compared to that of the crude extract. The optimal temperature for free α-amylase is 50˚C, while the optimum temperature for α-amylase/bentonite/chitosan is 60˚C. The KM value of α-amylase/bentonite/chitosan was 1.69 ± 0.08 mg mL-1 substrate and the Vmax value was 52.32 ± 3.29 µmol mL-1 min-1, whereas for free α-amylase, the KM value of 2.56 ± 0.09 mg mL-1 substrate and the Vmax value of 3.78 ± 0.09 µmol mL-1 min-1 were obtained. The ΔGi value of free α-amylase is 102.68 ± 0.30 kJ mol-1 and the t½ is 21.23 ± 0.23 min, whereas the ΔGi value of α-amylase/bentonite/chitosan is 104.43 ± 0.00 kJ mol-1 and the t½ is 94.29 ± 0.91 min. The higher values of ΔGi and t½demonstrated that α-amylase/bentonite/chitosan has better stability than that of free α-amylase. Another important finding is that α-amylase /bentonite/chitosan was able to retain their activity as high as 47.61 ± 0.53% after six recycles, indicating that the enzyme has the potential to be used in industry. Doi: 10.28991/ESJ-2023-07-05-023 Full Text: PDF

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Emerging Science Journal

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