Abstract
Starch—a mixture of amylose and amylopectin—serves as a food reserve for plants and provides a mechanism by which non-photosynthesizing organisms can utilize the energy provided by the sun. To utilize starch, the organisms must have enzymes that catalyze the hydrolysis of the (l→4) glycosidic bonds found between the α-D-glucopyranose residues. Enzymes that are capable of catalyzing the hydrolysis of the α-D-(l→4) linkages are called amylases, which are produced by plants, bacteria, and animals. In addition to the amylases, there are isoamylases or debranching enzymes that hydrolyze the α-D-(l→6) linkages of amylopectin. A number of analytical techniques have been devised for measuring the hydrolysis of glycosidic bonds found in starch. The most quantitative procedures involve the measurement of the formation of new reducing groups, hemiacetal or aldehyde groups, that result from the hydrolysis of the glycosidic, acetal, linkage.
Sign-in/Register to access full text options 
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.
