a Department of Biology Agriculture and Food Sciences , Institute of Bioscience and BioResources - National Research Council of Italy , Naples , Italy.
b Neurofarba Department , University of Florence, Polo Scientifico , Sesto Fiorentino Firenze , Italy.
J Enzyme Inhib Med Chem. 2019 Dec;34(1):946-954. doi: 10.1080/14756366.2019.1605991.
Carbonic anhydrases (CAs, EC 4.2.1.1) are a superfamily of ubiquitous metalloenzymes present in all living organisms on the planet. They are classified into seven genetically distinct families and catalyse the hydration reaction of carbon dioxide to bicarbonate and protons, as well as the opposite reaction. CAs were proposed to be used for biotechnological applications, such as the post-combustion carbon capture processes. In this context, there is a great interest in searching CAs with robust chemical and physical properties. Here, we describe the enhancement of thermostability of the α-CA from Sulfurihydrogenibium yellowstonense (SspCA) by using the anchoring-and-self-labelling-protein-tag system (ASL). The anchored chimeric H-SspCA was active for the CO hydration reaction and its thermostability increased when the cells were heated for a prolonged period at high temperatures (e.g. 70 °C). The ASL can be considered as a useful method for enhancing the thermostability of a protein useful for biotechnological applications, which often need harsh operating conditions.
碳酸酐酶（CA，EC 4.2.1.1）是一种广泛存在于地球上所有生物中的金属酶超家族。它们被分为七个具有遗传差异的家族，催化二氧化碳的水合反应生成碳酸氢盐和质子，以及相反的反应。CA 被提议用于生物技术应用，如燃烧后碳捕获过程。在这种情况下，人们对寻找具有稳健化学和物理性质的 CA 产生了浓厚的兴趣。在这里，我们描述了使用锚固和自标记蛋白标签系统（ASL）来增强来自 Sulfurihydrogenibium yellowstonense（SspCA）的α-CA 的热稳定性。锚定的嵌合 H-SspCA 对 CO 水合反应具有活性，并且当细胞在高温下长时间加热时，其热稳定性增加（例如 70°C）。ASL 可被视为增强用于生物技术应用的蛋白质热稳定性的有用方法，因为生物技术应用通常需要苛刻的操作条件。
