Enzyme and Microbial Biochemistry Laboratory, Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.
Food and Engineering Department, Institute of Chemical Technology, Matunga, Mumbai, India.
Bioresour Technol. 2021 Nov;339:125599. doi: 10.1016/j.biortech.2021.125599. Epub 2021 Jul 17.
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 V, K, 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.
L-天冬酰胺酶作为一种食品酶，具有很大的潜力，可以减少油炸和烘焙产品中丙烯酰胺的形成。但是对于食品应用，酶必须在高温下稳定，并且具有更高的催化效率。这些理想的特性是通过将酶固定在合适的基质上来赋予的。本研究旨在将 L-天冬酰胺酶固定在磁性纳米颗粒上，以降低食品体系中的丙烯酰胺含量。使用 SEM、TEM、FTIR、UV 光谱和 XRD 衍射分析对固定化制剂进行了表征。与游离酶相比，这些纳米颗粒将酶的热稳定性提高了四倍，在 70°C 下提高了四倍。动力学参数显示，V、K 和催化效率比游离酶提高了约 38%。固定化制剂可重复使用多达五轮。此外，它们在与漂烫相结合的土豆片预处理中的应用导致丙烯酰胺形成的显著减少（大于 95%）。
