Li Ran, Zhang Zehua, Pei Xiaomei, Xia Xiaole
The Key Laboratory of Industrial Biotechnology, School of Biotechnology, Jiangnan University, Wuxi, China.
Front Bioeng Biotechnol. 2020 Oct 15;8:584758. doi: 10.3389/fbioe.2020.584758. eCollection 2020.
Acrylamide is a potent carcinogen and neurotoxin that is mainly formed by the Maillard reaction of asparagine with starch at high temperatures. In this work, a food safety immobilization system for L-asparaginase (L-ASNase) consisting of food-grade agarose (Aga) spheres and N-hydroxysuccinimide esters was developed to decrease the formation of acrylamide in a fluid food model system. L-asparaginase was successfully immobilized with a maximum immobilization efficiency of 68.43%. The immobilized enzymes exhibited superior storage stability and reusability with 93.21 and 72.25% of the initial activity retained after six consecutive cycles and storage for 28 days, indicating its high industrial application potential. Meanwhile, a simplified mathematical model of the enzyme reactor was developed and verified with experiments, which demonstrated its auxiliary role in the design and optimization of reactors. In addition, simulated fluidized food components were continuously catalyzed in the designed packed bed reactor, achieving a reduction rate of nearly 89%.
丙烯酰胺是一种强效致癌物和神经毒素，主要由天冬酰胺与淀粉在高温下发生美拉德反应形成。在这项工作中，开发了一种由食品级琼脂糖（Aga）微球和N-羟基琥珀酰亚胺酯组成的用于L-天冬酰胺酶（L-ASNase）的食品安全固定化系统，以减少流体食品模型系统中丙烯酰胺的形成。L-天冬酰胺酶成功固定化，最大固定化效率为68.43%。固定化酶表现出优异的储存稳定性和可重复使用性，在连续六个循环和储存28天后分别保留了93.21%和72.25%的初始活性，表明其具有很高的工业应用潜力。同时，开发了酶反应器的简化数学模型并通过实验进行了验证，证明了其在反应器设计和优化中的辅助作用。此外，在设计的填充床反应器中对模拟的流体食品成分进行了连续催化，实现了近89%的降低率。
