丙烯酰胺
化学
固定化酶
热稳定性
纳米颗粒
磁性纳米粒子
漂白
酶
动力学
核化学
傅里叶变换红外光谱
化学工程
催化作用
色谱法
材料科学
有机化学
纳米技术
食品科学
聚合物
共聚物
工程类
物理
量子力学
作者
Shahenvaz Alam,Tanya Nagpal,Rekha S. Singhal,Sunil Kumar Khare
标识
DOI:10.1016/j.biortech.2021.125599
摘要
L-asparaginase shows great potential as a food enzyme to reduce acrylamide formation in fried and baked products. But for food applications, enzymes must be stable at high temperatures and have higher catalytic efficiency. These desirable characteristics are conferred by the immobilization of enzymes on a suitable matrix. The present study aimed to immobilize the L-asparaginase enzyme on magnetic nanoparticles to reduce acrylamide content in the food system. Immobilized preparations were characterized using SEM, TEM, FTIR, UV-spectrometry, and XRD diffraction analyses. These nanoparticles enhanced the thermal stability of the enzyme up to four-fold at 70 °C compared to the free enzyme. Kinetic parameters exhibited an increase in Vmax, Km, and catalytic efficiency by ~ 38% than the free counterpart. The immobilized preparations were reusable for up to five cycles. Moreover, their application in the pre-treatment coupled with blanching of potato chips led to a significant reduction (greater than 95%) of acrylamide formation.
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