AI Article Synopsis
- Starch-converting α-glucanotransferases from glycoside hydrolase family 70, like the novel GtfB enzyme WcMBF8-1, are valuable for creating various α-glucans for commercial use in food, health, and biomaterials.
- WcMBF8-1 GtfB showed unique variations in substrate-binding compared to other GtfB enzymes and demonstrated unusual 4,6-α-glucanotransferase activity, allowing it to alter starch linkages.
- The enzyme increased the amounts of slowly digestible and resistant starch in granular corn starch by 6.7%, indicating its potential for developing enhanced, clean-label starch products.
Article Abstract
Starch-converting α-glucanotransferases of glycoside hydrolase family 70 (GH70) are promising enzymatic tools for the production of diverse α-glucans with (potential) commercial applications in food and health and as biomaterials. In this study, a novel GtfB enzyme from MBF8-1 was screened in the National Center for Biotechnology Information (NCBI) nonredundant protein database. The enzyme (named WcMBF8-1 GtfB) displayed high conservation in motifs I-IV with other GtfB enzymes but possessed unique variations in several substrate-binding residues. Structural characterizations of its α-glucan products revealed that WcMBF8-1 GtfB exhibited an atypical 4,6-α-glucanotransferase activity and was capable of catalyzing, by cleaving off (α1 → 4)-linkages in starch-like substrates and the synthesis of linear (α1 → 6) linkages and (α1 → 4,6) branching points. The product specificity enlarges the diversity of α-glucans and facilitates recognition of the determinants of the linkage specificity in GtfB enzymes. Furthermore, the contents of slowly digestible starch and resistant starch of granular corn starches, modified by WcMBF8-1 GtfB, increased by 6.7%, which suggested the potential value for the utilization of WcMBF8-1 GtfB to prepare "clean-label" starch ingredients with improved functional attributes.
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