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Aspergillus oryzae β-D-galactosidase immobilization on glutaraldehyde pre-activated amino-functionalized magnetic mesoporous silica: Performance, characteristics, and application in the preparation of sesaminol

文献类型： 外文期刊

作者： Gao, Jinhong 1 ; Zhang, Lingli 2 ; Zhao, Dongxin 4 ; Lu, Xin 3 ; Sun, Qiang 3 ; Du, Heng 1 ; Yang, Hongyan 1 ; Lu, Kui 1 ;

作者机构： 1.Henan Univ Technol, Coll Food Sci & Engn, Zhengzhou 450044, Henan, Peoples R China

2.Zhengzhou Univ Technol, Sch Chem Engn & Food Sci, Zhengzhou 450044, Henan, Peoples R China

3.Henan Acad Agr Sci, Res Ctr Agr & Sideline Prod Proc, Zhengzhou 450044, Henan, Peoples R China

4.Henan Univ Technol, Sch Chem & Chem Engn, Lianhua Rd 100, Zhengzhou 450001, Henan, Peoples R China

关键词： Aspergillus oryzae; beta-D-galactosidase; Magnetic mesoporous silica; Enzyme immobilization; Glutaraldehyde; Sesaminol

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2024 年 270 卷

页码：

收录情况： SCI

摘要： Aspergillus oryzae beta- D-galactosidase ( beta- Gal) efficiently hydrolyzes sesaminol triglucoside into sesaminol, which has higher biological activity. However, beta- Gal is difficult to be separate from the reaction mixture and limited by stability. To resolve these problems, beta- Gal was immobilized on amino-functionalized magnetic nanoparticles mesoporous silica pre -activated with glutaraldehyde (Fe 3 O 4 @mSiO 2 - beta- Gal), which was used for the first time to prepare sesaminol. Under the optimal conditions, the immobilization yield and recovered activity of beta- Gal were 57.9 +/- 0.3 % and 46.5 +/- 0.9 %, and the enzymatic loading was 843 +/- 21 U enzyme /g support . The construction of Fe 3 O 4 @mSiO 2 - beta- Gal was confirmed by various characterization methods, and the results indicated it was suitable for heterogeneous enzyme -catalyzed reactions. Fe 3 O 4 @mSiO 2 - beta- Gal was readily separable under magnetic action and displayed improved activity in extreme pH and temperature conditions. After 45 days of storage at 4 degrees C, the activity of Fe 3 O 4 @mSiO 2 - beta- Gal remained at 92.3 +/- 2.8 %, which was 1.29 times than that of free enzyme, and its activity remained above 85 % after 10 cycles. Fe 3 O 4 @mSiO 2 - beta- Gal displayed higher affinity and catalytic efficiency. The half-life was 1.41 longer than free enzymes at 55.0 degrees C. Fe 3 O 4 @mSiO 2 - beta- Gal was employed as a catalyst to prepare sesaminol, achieving a 96.7 % conversion yield of sesaminol. The excellent stability and catalytic efficiency provide broad benefits and potential for biocatalytic industry applications.

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