Abstract
Amylomaltases or D-enzyme (4-α-glucanotransferases; E.C. 2.4.1.25) are carbohydrate-active enzymes that catalyze the transfer of glucan units from one α-glucan to another in a disproportionation reaction. These enzymes are involved in starch metabolism in plants or maltose/glycogen metabolism in many microorganisms. The amylomaltase of the hyperthermophilic bacterium Thermus thermophilus HB8 was overproduced in Escherichia coli, partially purified and used to modify potato starch. The action of amylomaltase caused the disappearance of amylose and the broadening of the side-chain length distribution in amylopectin, which resulted in a product with both shorter and longer side chains than in the parent starch. Amylomaltase-treated potato starch showed thermoreversible gelation at concentrations of 3% (w/v) or more, thus making it comparable to gelatin. Because of its animal origin, gelatin is not accepted by several consumer groups. Therefore, the amylomaltase-treated potato starch might be a good plant-derived substitute for gelatin.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
