来源于[具体来源未给出]的鸟嘌呤脱氨酶的特性及其在降低啤酒中鸟嘌呤含量方面的工业应用。
Characterization of Guanine Deaminase from and Its Industrial Application to Reduce Guanine Content in Beer.
作者信息
Zhou Peng, Xu Junhao, Wang Zixuan, Li Baoguo, Zhao Zhijun
机构信息
School of Health Science and Engineering, University of Shanghai for Science and Technology, Shanghai 200120, China.
Laboratory of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 200120, China.
出版信息
Foods. 2025 Mar 21;14(7):1085. doi: 10.3390/foods14071085.
Guanine deaminase (GDA) catalyzes the first step in purine catabolism by converting guanine to xanthine. Despite its significant role in the development of low-purine food, studies on GDA remain limited compared to other metabolic deaminases. To identify a GDA with high enzyme activity and appropriate optimum parameters, GDAs from , , , and were heterologously expressed in . The GDA from (KM-GD) showed the most potent enzyme activity (2.21 IU/mL) at 30 °C and pH 6.5, which is close to the pH of saccharified wort. Furthermore, analyzing the crystal structures of GDAs from different sources revealed that hydrogen bonds could enhance substrate affinity and strengthen enzyme activity. In addition, active pockets with an appropriate size may contribute to high enzyme activity. Finally, KM-GD helped reduce guanine by 80.33% in beer wort and by 80.00% in matured beer, thus suggesting its promise for industrial application in low-purine food production.
鸟嘌呤脱氨酶（GDA）通过将鸟嘌呤转化为黄嘌呤来催化嘌呤分解代谢的第一步。尽管其在低嘌呤食品开发中具有重要作用，但与其他代谢脱氨酶相比，关于GDA的研究仍然有限。为了鉴定具有高酶活性和合适最佳参数的GDA，来自[具体来源1]、[具体来源2]、[具体来源3]和[具体来源4]的GDA在[表达宿主]中进行了异源表达。来自[具体来源5]的GDA（KM-GD）在30°C和pH 6.5时表现出最强的酶活性（2.21 IU/mL），这接近糖化麦芽汁的pH值。此外，对不同来源GDA的晶体结构分析表明，氢键可以增强底物亲和力并增强酶活性。此外，具有合适大小的活性口袋可能有助于提高酶活性。最后，KM-GD在啤酒麦芽汁中使鸟嘌呤减少了80.33%，在成熟啤酒中减少了80.00%，因此表明其在低嘌呤食品生产中的工业应用前景。
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