1982•Starch - StärkeRequires access

The Possible Relationship of Starch and Phytoglycogen in Sweet Corn. II. The Role of Branching Enzyme I

Charles D. Boyer, E. K. G. Simpson, P. A. Damewood

Open publisher page 32 citations

Abstract

Abstract Developing maize kernels contain three starch branching enzymes. Homogeneous branching enzyme I has now been shown to be capable of branching amylose as well as amylopectin but not glycogens. The formation of glycogen‐like molecules by the further branching of amylopectin suggests that branching enzyme I plays a role in phytoglycogen formation. Its presence in nonmutant kernels which do not accumulate phytoglycogen, however, indicates that amylopectin per se is not accessible to branching enzyme I for phytoglycogen formation. Treatment of sugary (su) starch granules with enzyme I resulted in soluble phytoglycogen‐like glucan. No glucan was released by treatment of nonmutant starch granules. In addition, nonsolublized amylopectin and amylose fractions of the su starch were branched during the incubations. These observations are consistent with plastid changes which show a conversion of starch granules to phytoglycogen in sugary endosperm cells.

About this research paper

What this paper is about

Abstract Developing maize kernels contain three starch branching enzymes. Homogeneous branching enzyme I has now been shown to be capable of branching amylose as well as amylopectin but not glycogens. The formation of glycogen‐like molecules by the further branching of amylopectin suggests that branching enzyme I plays a role in phytoglycogen formation. Its presence in nonmutant kernels which do not accumulate phytoglycogen, however, indicates that amylopectin per se is not accessible to branching enzyme I for phytoglycogen formation. Treatment of sugary (su) starch granules with enzyme I resulted in soluble phytoglycogen‐like glucan. No glucan was released by treatment of nonmutant starch granules. In addition, nonsolublized amylopectin and amylose fractions of the su starch were branched during the incubations. These observations are consistent with plastid changes which show a conversion of starch granules to phytoglycogen in sugary endosperm cells.

Why it matters

OpenAlex reports 32 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Abstract Developing maize kernels contain three starch branching enzymes. Homogeneous branching enzyme I has now been shown to be capable of branching amylose as well as amylopectin but not glycogens. The formation of glycogen‐like molecules by the further branching of amylopectin suggests that branching enzyme I plays a role in phytoglycogen formation. Its presence in nonmutant kernels which do not accumulate phytoglycogen, however, indicates that amylopectin per se is not accessible to branching enzyme I for phytoglycogen formation. Treatment of sugary (su) starch granules with enzyme I resulted in soluble phytoglycogen‐like glucan. No glucan was released by treatment of nonmutant starch granules. In addition, nonsolublized amylopectin and amylose fractions of the su starch were branched during the incubations. These observations are consistent with plastid changes which show a conversion of starch granules to phytoglycogen in sugary endosperm cells.

Key concepts: Amylopectin, Endosperm, Amylose, Glycogen branching enzyme, Glycogen debranching enzyme, Starch, Branching (polymer chemistry), Chemistry

Related papers

Back to paper searchBrowse research topicsOriginal source
The Possible Relationship of Starch and Phytoglycogen in Sweet Corn. II. The Role of Branching Enzyme I — Research Paper | ScholarLens