Thermostability enhancement of the α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense by using the anchoring-and-self-labelling-protein-tag system (ASLtag)

• मुख्य लेखकों: Sonia Del Prete (लेखक), Rosa Merlo (लेखक), Anna Valenti (लेखक), Rosanna Mattossovich (लेखक), Mosè Rossi (लेखक), Vincenzo Carginale (लेखक), Claudiu T. Supuran (लेखक), Giuseppe Perugino (लेखक), Clemente Capasso (लेखक)
• स्वरूप: पुस्तक
• प्रकाशित: Taylor & Francis Group, 2019-01-01T00:00:00Z.
• विषय: article
• ऑनलाइन पहुंच: Connect to this object online.
• Notes: 1475-6366; 1475-6374; 10.1080/14756366.2019.1605991
• Keywords: carbonic anhydrase; thermostability; sulfurihydrogenibium yellowstonens; alkylguanine-dna-alkyl-transferase; asltag; Therapeutics. Pharmacology; RM1-950
• Source: Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 946-954 (2019)

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 (ASLtag). The anchored chimeric H5-SspCA was active for the CO2 hydration reaction and its thermostability increased when the cells were heated for a prolonged period at high temperatures (e.g. 70 °C). The ASLtag can be considered as a useful method for enhancing the thermostability of a protein useful for biotechnological applications, which often need harsh operating conditions.