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来源于[具体来源未提及]的尿酸酶,一种降低豆制品尿酸含量的工业应用候选物。

Uricase from , a Candidate for Industrial Application of Reducing Uric Acid Content of Bean Products.

作者信息

Zhou Peng, Zhu Chengzhi, Zou Yijun, Li Baoguo, Zhao Zhijun

机构信息

School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China.

Lab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Shanghai 201210, China.

出版信息

J Agric Food Chem. 2025 Jan 15;73(2):1441-1448. doi: 10.1021/acs.jafc.4c05973. Epub 2025 Jan 2.

Abstract

Microbial uricase is an essential enzyme in purine degradation and the development of low-purine food. High enzyme activity and an appropriate optimum pH must be established for low-purine food. Uricases from , , , , and were heterologously expressed in . Uricase from (AC-PUCL) showed the most potent enzyme activity (249.19 IU/mL) at 37 °C and pH 7.0. This is close to the pH of plant-based food. The and / values of AC-PUCL were 30.12 μM and 1.46 s μM, respectively. Furthermore, the crystal structures of uricases from different sources revealed that hydrogen bonds could enhance substrate affinity and strong enzyme activity. In addition, the high enzyme activity may be contributed by the active pockets with an appropriate size. Finally, AC-PUCL helped reduce the purine substances in soybean, pea, and kidney bean, with residual uric acid can not be detected at pH 8.6, suggesting a promising industrial application.

摘要

微生物尿酸酶是嘌呤降解和低嘌呤食品开发中的一种关键酶。低嘌呤食品必须具备高酶活性和合适的最适pH值。来自[具体物种1]、[具体物种2]、[具体物种3]、[具体物种4]和[具体物种5]的尿酸酶在[表达宿主]中进行了异源表达。来自[具体物种6]的尿酸酶(AC-PUCL)在37℃和pH 7.0时表现出最强的酶活性(249.19 IU/mL)。这接近植物性食品的pH值。AC-PUCL的Km和kcat/Km值分别为30.12μM和1.46 s-1μM。此外,不同来源尿酸酶的晶体结构表明,氢键可增强底物亲和力和强大的酶活性。此外,高酶活性可能由具有合适大小的活性口袋所致。最后,AC-PUCL有助于降低大豆、豌豆和菜豆中的嘌呤物质,在pH 8.6时未检测到残留尿酸,表明其具有广阔的工业应用前景。

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