Covalent immobilization of recombinant L-asparaginase from Geobacillus kaustophilus on ReliZyme supports for mitigation of acrylamide

被引：3
作者：
Ozdemir, F. Inci [1 ,4 ]
Karaaslan, Burcu [1 ]
Tulek, Ahmet [2 ]
Yildirim, Deniz [3 ]
机构：
[1] Gebze Tech Univ, Fac Sci, Dept Mol Biol & Genet, Gebze, Kocaeli, Turkiye
[2] Igdir Univ, Dept Bioengn & Sci, Merkez, Igdir, Turkiye
[3] Cukurova Univ, Fac Ceyhan Engn, Dept Chem Engn, Ceyhan, Adana, Turkiye
[4] Gebze Tech Univ, Fac Sci, Dept Mol Biol & Genet, TR-41400 Gebze, Kocaeli, Turkiye
来源：
BIOCATALYSIS AND BIOTRANSFORMATION | 2024年 / 42卷 / 03期
关键词：
Geobacillus kaustophilus; L-asparaginase; ReliZyme; acrylamide mitigation; STRATEGIES; SEPABEADS; GLUTARALDEHYDE; STABILIZATION; REDUCTION; DESIGN; FOOD;
D O I：
10.1080/10242422.2023.2257351
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
In this study, a new recombinant L-asparaginase from Geobacillus kaustophilus was covalently immobilized on ReliZyme EA403 (Relizyme/EA@GkASNase) and ReliZyme HA403 (Relizyme/HA@GkASNase) supports, and the free and immobilized L-asparaginases were used for their acrylamide mitigation performances in a food model system. The immobilization was confirmed by fourier-transform infrared spectroscopy, scanning electron microscopy, and transmission electron microscopy analysis. The optimum pH was determined as 8.5 for all the free and immobilized L-asparaginase samples. The optimum temperature was determined as 55 ? for the free enzyme and 60 ? for both the immobilized samples. The thermal stability of L-asparaginase was increased by 17.6 and 37.2 folds at 60 ? for Relizyme/EA@GkASNase and Relizyme/HA@GkASNase, respectively. Relizyme/EA@GkASNase and Relizyme/HA@GkASNase showed 16% and 43% of the catalytic efficiency of free GkASNase. The acrylamide mitigation performances of free and immobilized L-asparaginase samples were investigated using the L-asparagine-starch food model system and the formed acrylamide was completely mitigated in 1 h for all the L-asparaginase samples. Both the immobilized L-asparaginase samples retained at least 80% of their activities after five reuses. Hence, the immobilized GkASNase preparations can be potentially used in heat-treated food industries to remove acrylamide.
引用
收藏
页码：426 / 439
页数：14
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