Lerner Aaron, Ramesh Ajay, Matthias Torsten
AESKU.KIPP Institute, Wendelsheim, Germany.
FEBS Open Bio. 2020 Apr;10(4):492-494. doi: 10.1002/2211-5463.12839.
Transglutaminases (TGs) play important roles in the food industry, pharmacology, and biotechnology, but as protein cross-linkers, their complexes are stable, resistant, immunogenic, and potentially pathogenic. Many TGs have been characterized, but they operate in narrow temperature and pH range limits. In a research article in this issue, Clemens Furnes and colleagues describe a novel cold-adapted TG from Atlantic cod, which expands the operating boundaries to a lower temperature and a wider pH. In this accompanying commentary, we discuss how this TG opens new applications in cold environments and can be deactivated by heating. New sources of TGs should be explored in hot environments like hot springs, in order to increase the temperature and widen the pH ranges for human and industrial benefits.
转谷氨酰胺酶(TGs)在食品工业、药理学和生物技术中发挥着重要作用,但作为蛋白质交联剂,它们形成的复合物稳定、抗逆、具有免疫原性且可能具有致病性。许多转谷氨酰胺酶已得到表征,但它们的作用温度和pH范围较窄。在本期的一篇研究文章中,克莱门斯·弗内斯及其同事描述了一种来自大西洋鳕鱼的新型冷适应性转谷氨酰胺酶,它将作用边界扩展到了更低的温度和更宽的pH范围。在这篇随附的评论中,我们讨论了这种转谷氨酰胺酶如何在寒冷环境中开辟新的应用,以及如何通过加热使其失活。为了人类和工业利益而提高温度和拓宽pH范围,应该在温泉等高温环境中探索转谷氨酰胺酶的新来源。