Optimization and characterization of immobilized thermostable α-amylase from germinating Sword bean (Canavalia gladiata (Jacq.) DC.) seeds on DEAE-cellulose and chitosan bead for operational stability.

IF 16.4 1区化学 Q1 CHEMISTRY, MULTIDISCIPLINARY Accounts of Chemical Research Pub Date : 2024-06-25 DOI:10.5511/plantbiotechnology.24.0326a

Saijai Posoongnoen, Sutthidech Preecharram, Jinda Jandaruang, Theera Thummavongsa

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Abstract

Thermostable α-amylase from germinating Sword bean (Canavalia gladiata (Jacq.) DC.) seeds has been successfully immobilized on DEAE-cellulose (ICgAmy1) and chitosan bead (ICgAmy2) support materials. Optimum conditions of immobilization for DEAE-cellulose and chitosan bead revealed 97% and 96% immobilization yield, respectively. The optimum pH and temperature of both DEAE-cellulose and chitosan bead immobilized α-amylases were pH 7 and 70°C. Both ICgAmy1 and ICgAmy2 were high stability over a wide pH range of pH 5-9 and a temperature range of 70-90°C. In addition, ICgAmy1 and ICgAmy2 led to an operationally stable biocatalyst with above 74% and 76% residual activity after 10 reuses, respectively. Immobilized α-amylases showed high storage stability with 81% (ICgAmy1) and 85% (ICgAmy2) residual activity after 120 days of storage. The easy immobilization process on low-cost, biodegradable, and renewable support materials exhibited an increase in the enzyme operation range and storage stability which reduces production costs. This makes immobilized amylases an effective biocatalyst in various industrial applications especially a potential candidate for bioethanol production, a key renewable energy source.

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从发芽剑豆（Canavalia gladiata (Jacq.) DC.）种子中提取的固定化恒温α-淀粉酶在 DEAE-纤维素和壳聚糖珠上的优化和表征，以确保其操作稳定性。

成功地将发芽剑豆（Canavalia gladiata (Jacq.) DC.）种子中的α-淀粉酶固定在DEAE-纤维素（ICgAmy1）和壳聚糖珠（ICgAmy2）支撑材料上。在 DEAE-纤维素和壳聚糖珠的最佳固定化条件下，固定化率分别为 97% 和 96%。DEAE-纤维素和壳聚糖珠固定化α-淀粉酶的最佳 pH 值和温度分别为 pH 7 和 70°C。ICgAmy1 和 ICgAmy2 在 pH 值 5-9 和 70-90°C 的较宽 pH 值范围内都具有较高的稳定性。此外，ICgAmy1 和 ICgAmy2 还产生了操作稳定的生物催化剂，在重复使用 10 次后，其残余活性分别超过 74% 和 76%。固定化的 α 淀粉酶具有很高的贮存稳定性，贮存 120 天后的残余活性分别为 81%（ICgAmy1）和 85%（ICgAmy2）。在低成本、可生物降解和可再生的支撑材料上进行简单的固定化处理，可提高酶的工作范围和储存稳定性，从而降低生产成本。这使得固定化淀粉酶成为各种工业应用中有效的生物催化剂，尤其是生物乙醇生产的潜在候选者，而生物乙醇是一种重要的可再生能源。

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来源期刊

Accounts of Chemical Research 化学-化学综合

CiteScore

31.40

自引率

1.10%

发文量

312

审稿时长

2 months

期刊介绍： Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.

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