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从发芽的刀豆（(Jacq.) DC.）种子中提取的热稳定α-淀粉酶固定于DEAE-纤维素和壳聚糖珠上的优化及表征，以实现操作稳定性。

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

作者信息

Posoongnoen Saijai, Preecharram Sutthidech, Jandaruang Jinda, Thummavongsa Theera

机构信息

Division of Chemistry, Faculty of Science and Technology, Nakhon Ratchasima Rajabhat University.

Department of General Science, Faculty of Science and Engineering, Kasetsart University Chalermphrakiat Sakon Nakhon Province Campus.

出版信息

Plant Biotechnol (Tokyo). 2024 Jun 25;41(2):129-136. doi: 10.5511/plantbiotechnology.24.0326a.

DOI:10.5511/plantbiotechnology.24.0326a
PMID:39463774
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11500564/
Abstract

Thermostable α-amylase from germinating Sword bean ( (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.

摘要

来自发芽刀豆（(Jacq.) DC.）种子的耐热α-淀粉酶已成功固定在DEAE-纤维素（ICgAmy1）和壳聚糖珠（ICgAmy2）载体材料上。DEAE-纤维素和壳聚糖珠的最佳固定化条件分别显示固定化产率为97%和96%。DEAE-纤维素和壳聚糖珠固定化α-淀粉酶的最佳pH值和温度均为pH 7和70°C。ICgAmy1和ICgAmy2在pH 5-9的宽pH范围内以及70-90°C的温度范围内均具有高稳定性。此外，ICgAmy1和ICgAmy2分别在重复使用10次后产生了具有74%以上和76%以上残余活性的操作稳定的生物催化剂。固定化α-淀粉酶在储存120天后显示出高储存稳定性，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载体材料上进行的简单固定化过程提高了酶的操作范围和储存稳定性，从而降低了生产成本。这使得固定化淀粉酶成为各种工业应用中的有效生物催化剂，尤其是生物乙醇生产的潜在候选者，生物乙醇是一种关键的可再生能源。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/b7c78eabf17a/plantbiotechnology-41-2-24.0326a-figure04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/e572073070cb/plantbiotechnology-41-2-24.0326a-figure01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/bf45bb066aab/plantbiotechnology-41-2-24.0326a-figure02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/0f52dd0fe70c/plantbiotechnology-41-2-24.0326a-figure03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/b7c78eabf17a/plantbiotechnology-41-2-24.0326a-figure04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/e572073070cb/plantbiotechnology-41-2-24.0326a-figure01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/bf45bb066aab/plantbiotechnology-41-2-24.0326a-figure02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/0f52dd0fe70c/plantbiotechnology-41-2-24.0326a-figure03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0de9/11500564/b7c78eabf17a/plantbiotechnology-41-2-24.0326a-figure04.jpg

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Purification and characterization of thermostable α-amylase from germinating Sword bean ( (Jacq.) DC.) seeds.发芽刀豆（Canavalia gladiata (Jacq.) DC.）种子中耐热α-淀粉酶的纯化与特性分析
Plant Biotechnol (Tokyo). 2020 Mar 25;37(1):31-38. doi: 10.5511/plantbiotechnology.19.1209b.
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