Immobilization of α-amylase on modified magnetic zeolite (MAZE) coated with carboxymethyl cellulose (CMC) composite and its properties

被引:19
作者
Azizi, Vali [1 ,2 ]
Mohammadi, Maryam [1 ,2 ]
Mokarram, Reza Rezaei [1 ]
Khiabani, Mahmood Sowti [1 ]
Hamishehkar, Hamed [2 ]
机构
[1] Univ Tabriz, Fac Agr, Dept Food Sci & Technol, Tabriz, Iran
[2] Tabriz Univ Med Sci, Drug Appl Res Ctr, Tabriz, Iran
关键词
Immobilization; alpha-Amylase; Magnetic nanoparticles; Zeolite; Covalent immobilization; OXIDE NANOPARTICLES; CATALYTIC-ACTIVITY; STABILITY; NANOCOMPOSITES; ENHANCEMENT; LIPASE; FE3O4; IMPROVEMENT; ENZYMES;
D O I
10.1016/j.lwt.2021.111214
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The enzyme immobilization process can address some problems associated with the free form (high price of enzyme production, difficulty in the separation of products from reaction media, and lack of reusability). In this study, alpha-amylase was covalently immobilized on the magnetic zeolite (MAZE) particles entrapped in the carboxymethyl cellulose (CMC) composite. The synthesized carrier and immobilized enzyme were fully characterized. The optimal temperature and pH for free enzyme were observed at 30 degrees C and 6.5, respectively. The optimal temperature for both forms of immobilized enzymes did not change after the immobilization process. The optimal pH for immobilized enzyme on MAZE particles had a shift towards basic region (pH 8). The immobilized enzyme into MAZE/CMC composite showed a broad optimum pH of 6.5-8.0 and high storage stability after 40 days of storage at 4 degrees C (78%). The reusability experiment indicated that approximately 45% of the initial activity of both immobilized enzymes remained after 12 times recycling. The K-m and V-max values were slightly changed after both immobilization processes. Finally, it can be proposed that the designed carrier in this study can be used in the industrial production of glucose syrup and electrochemical sensors.
引用
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页数:10
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