Liu Fuhao, Zheng Xiangnan, Liao Wenhui, Ren Xingtao, Ma Chuanteng, Zhang Guojian, Che Qian, Zhu Tianjiao, Wang Wenxue, Zhang Tao, Han Feng, Li Dehai
Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, 5 Yushan Road, Qingdao 266003, China.
Laboratory for Marine Drugs and Bioproducts, Qingdao Marine Science and Technology Center, Qingdao 266237, China.
Mar Drugs. 2025 Apr 4;23(4):159. doi: 10.3390/md23040159.
α-Amylases, catalyzing starch degradation, serve as vital biocatalysts in industrial and pharmaceutical applications. This study identified a new α-amylase, Alphaz, from HDN19-252 of Antarctic animal origin, achieving heterologous expression in . Phylogenetic analysis confirmed its classification into the GH13_5 subfamily of glycoside hydrolases. Recombinant Alphaz exhibited optimal activity at 40 °C/pH 8.0 while maintaining stability across 0-30 °C and pH 6.6-9.6. Its distinctive halotolerant properties included full activity retention in 0.6 M NaCl and >60% efficiency in salt-free conditions. The enzyme exhibits tolerance to K, Ca, and Fe³ while demonstrating specific inhibition by Cu/Zn. With its heterologously validated functional properties, Alphaz emerges as a programmable enzymatic tool offering advantages in sustained-release formulation quality control, targeted prodrug modification, and precision medicine applications, thereby enabling sustainable biomanufacturing solutions that harmonize process reliability with environmental compatibility.
α-淀粉酶催化淀粉降解，在工业和制药应用中作为重要的生物催化剂。本研究从南极动物来源的HDN19-252中鉴定出一种新的α-淀粉酶Alphaz，并在……中实现了异源表达。系统发育分析证实其属于糖苷水解酶的GH13_5亚家族。重组Alphaz在40°C/pH 8.0时表现出最佳活性，同时在0-30°C和pH 6.6-9.6范围内保持稳定。其独特的耐盐特性包括在0.6 M NaCl中完全保留活性，在无盐条件下效率>60%。该酶对K、Ca和Fe³具有耐受性，同时表现出对Cu/Zn的特异性抑制。凭借其经过异源验证的功能特性，Alphaz成为一种可编程的酶工具，在缓释制剂质量控制、靶向前药修饰和精准医学应用中具有优势，从而实现了将工艺可靠性与环境兼容性相协调的可持续生物制造解决方案。
