Biochemical and Biophysical Research Communications
Multiple forms of starch branching enzyme of maize: Evidence for independent genetic control
References (14)
- et al.
J. Biol. Chem
(1949) - et al.
Arch. Biochem. Biophys
(1974) - et al.
J. Biol. Chem
(1951) Anal. Biochem
(1962)- et al.
Biochim. Biophys. Acta
(1969) - et al.
FEBS lett
(1970) - et al.
Arch. Biochem. Biophys
(1974)
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The effect of amylose on kernel phenotypic characteristics, starch-related gene expression and amylose inheritance in naturally mutated high-amylose maize
2020, Journal of Integrative AgriculturePlant Starch Synthesis
2018, Starch in Food: Structure, Function and Applications: Second EditionCritical and speculative review of the roles of multi-protein complexes in starch biosynthesis in cereals
2017, Plant ScienceCitation Excerpt :In this review, we described protein–protein interactions in cereal endosperm between starch biosynthetic enzymes, including SSs, starch branching enzymes (BEs), starch debranching enzymes, and plastidial Pho1. The formation of protein–protein complexes for starch biosynthesis has been suggested in biochemical studies of enzymes from developing wild-type and mutant maize kernels after chromatographic fractionation [14–16]. Moreover, direct evidence of phosphorylation-dependent multi-enzyme complex formation in starch biosynthesis was first shown in developing wheat endosperm [17].
Plant Starch Synthesis
2017, Starch in Food: Structure, Function and ApplicationsImproving cereal grain carbohydrates for diet and health
2014, Journal of Cereal ScienceCitation Excerpt :There is a marked decrease in the proportion of chain lengths of DP 4–12 and a corresponding increase in the chain lengths greater than DP 12. Whereas no effect is associated with the loss of expression of SBEIIb in wheat (Regina et al., 2006; Sestili et al., 2010b), the absence of expression in maize and rice results in a phenotype, designated as amylose extender (ae) (Mizuno et al., 1993; Boyer and Preiss, 1978), with a profound effect on the amount of amylose and the structure of amylopectin. It should be stressed that reduction or elimination of starch branching enzyme activity will not result in the production of true amylose; the major effect will be the reduction of branch points in the amylopectin fraction that will result in the formation of an amylopectin polymer with amylose-like properties (Morell et al., 2004).
Characterization of substrate and product specificity of the purified recombinant glycogen branching enzyme of Rhodothermus obamensis
2013, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :Alternatively, this band may correspond to contaminating proteins co-purified with RoBE but without any glucan-modifying/degrading activity. Subsequently, the specific activity of the recombinant enzyme was estimated by an in vitro assay following a previously described method [24] and at 30 °C and pH 7, which does not correspond to the optimal temperature and pH as previously described [19]. Such suboptimal conditions were selected in the future perspective to combine RoBE activity with other non-thermostable enzymes for the in vitro production of new polymers from low-cost renewable resources.