Abstract Enzyme immobilization is a routine biotechnology of many industries such as pharmaceutical, chemical and food. Among the different techniques of enzyme immobilization, cross-linking methods are often used. Geniposide is a natural product extracted from gardenia and its hydrolysate genipin is one of green cross-linking agent for enzyme immobilization, but the environmental pollution and cost of the genipin extraction process have become the main obstacle to its wide application. Enzyme β-glucosidase was immobilized on chitosan by self-catalysis and further used to hydrolyze geniposide. The laccase was immobilized on Nano-SiO2 through the hydrolysate of geniposide directly acts as cross-linking agent. The simplification of the extraction steps overcomes the obstacles to the widespread use of genipin. Compared with the free laccase, the Nano-SiO2@laccase exhibited better pH stability and thermal stability. The Nano-SiO2@laccase was used to degrade Bisphenol A (BPA) and the biodegradation efficiency of the Nano-SiO2@laccase was 84.3 % after 10 cycles of reusing.

中文翻译：

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栀子苷酶水解物直接作为酶固定化的交联剂

摘要 酶固定化是制药、化工、食品等诸多行业的常规生物技术。在酶固定化的不同技术中，经常使用交联方法。栀子苷是从栀子中提取的天然产物，其水解物京尼平是一种绿色的酶固定化交联剂，但京尼平提取过程的环境污染和成本已成为其广泛应用的主要障碍。酶β-葡萄糖苷酶通过自催化固定在壳聚糖上并进一步用于水解栀子苷。漆酶通过栀子苷水解产物直接作为交联剂固定在纳米二氧化硅上。提取步骤的简化克服了京尼平广泛使用的障碍。与游离漆酶相比，Nano-SiO2@laccase 表现出更好的 pH 稳定性和热稳定性。Nano-SiO2@laccase 用于降解双酚 A (BPA)，Nano-SiO2@laccase 在重复使用 10 次后的生物降解效率为 84.3%。