Different isoforms of starch-synthesizing enzymes controlling amylose and amylopectin content in rice (Oryza sativa L.)
- PMID: 22960619
- DOI: 10.1016/j.biotechadv.2012.08.011
Different isoforms of starch-synthesizing enzymes controlling amylose and amylopectin content in rice (Oryza sativa L.)
Abstract
Starch, composed of amylose and amylopectin, greatly influences rice cooking and textural quality, which in turn is controlled by various isoforms of several enzymes. Activity of one or more isoforms of starch-synthesizing enzymes results in various forms of starch structure based on the amylopectin chain length and average external, internal and core chain length distribution and hence results in varying physicochemical and cooking quality. Since the synthesis of starch is highly complex, it is crucial but essential to understand its biosynthetic pathway, starch structure and effects on the physicochemical properties that control eating and cooking quality, and alongside conduct research on gene/QTL mapping for use in marker-assisted selection (MAS) with a view to improve and select cultivars with most desirable range and class of rice starch properties. This article presents the updates on current understanding of the coordination among various enzymes/isoforms towards rice starch synthesis in endosperm and their effect on rice grain physicochemical, cooking and eating qualities. The efforts in identifying regions responsible for these enzymes by mapping the gene/QTLs have provided a glimpse on their association with physicochemical and cooking properties of rice and, hence, improvement is possible by modifying the allelic pattern, resulting in down or nil regulation of a particular enzyme. The clear understanding of the tissue specific coordination between enzyme isoforms and their subsequent effect in controlling eating and cooking properties will enhance the chances to manipulate them for getting desired range of amylose content (AC) and gelatinization temperature (GT) in improved cultivars through combining desired alleles through MAS.
Copyright © 2012 Elsevier Inc. All rights reserved.
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