Presents a novel CGTase from Haloferax sp. that efficiently degrades starch, suggesting its potential in various applications.
Cyclodextrin glycosyltransferase (CGTase) is a highly valuable biocatalyst in industrial starch conversion, particularly for the synthesis of cyclic oligosaccharides. In this study, a CGTase, designated HfCGT, was cloned from Haloferax sp. and heterologously expressed in Escherichia coli. The recombinant enzyme was purified and biochemically characterized. HfCGT exhibited maximal catalytic activity at 70 °C and pH 8.0, tolerance to metal ions and EDTA, and enhanced activity in the presence of 1 M NaCl and Ca2+. High-performance liquid chromatography (HPLC) and high-resolution mass spectrometry (HRMS) analyses revealed that the starch products by HfCGT degradation were mainly large-ring cyclodextrins (LR-CDs) with polymerization degrees of 9 to 20. Altogether, the thermostability, haloalkaliphilic, and distinctive product profile make HfCGT a promising biocatalyst for pharmaceutical, food, and biotechnological applications.
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Li et al. (2026) studied this question.
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