Progress in Controlling Starch Structure by Modifying Starch-branching Enzymes

Overview

Journal Planta

Specialty Biology

Date 2015 Oct 22

PMID 26486516

Citations 12

Authors

Cheng Li

Robert G Gilbert

Affiliations

Soon will be listed here.

Abstract

This paper reviews the progress of development of plants with desirable starch structure by modifying starch branching enzymes. Starch-branching enzyme (SBE) is responsible for the creation of branches during starch biosynthesis in plastids, and is a major determinant of the final fine structure and physical properties of the starch. Multiple isoforms of SBE have been found in plants, with each playing a different role in amylopectin synthesis. Different methods have been used to develop desirable starch structures by modifying the SBE activity. These can involve changing its expression level (either up-regulation or down-regulation), genetically modifying the activity of the SBE itself, and varying the length of its transferred chains. Changing the activity and the transferred chain length of SBE has been less studied than changing the expression level of SBE in vivo. This article reviews and summarizes new tools for developing plants producing the next generation of starches.

Citing Articles

Preparation of Neohesperidin-Taro Starch Complex as a Novel Approach to Modulate the Physicochemical Properties, Structure and In Vitro Digestibility.

Zuo Y, He Z, Yang W, Sun C, Ye X, Tian J Molecules. 2023; 28(9).

PMID: 37175311 PMC: 10179776. DOI: 10.3390/molecules28093901.

Disentangling the resistant mechanism of Fusarium wilt TR4 interactions with different cultivars and its elicitor application.

Zhou G, He P, Tian L, Xu S, Yang B, Liu L Front Plant Sci. 2023; 14:1145837.

PMID: 36938065 PMC: 10018200. DOI: 10.3389/fpls.2023.1145837.

Preparation and Characterization of Extruded Yam Starch-Soy Protein Isolate Complexes and Their Effects on the Quality of Dough.

Shi M, Dong X, Cheng Y, Ji X, Liu Y, Yan Y Foods. 2023; 12(2).

PMID: 36673452 PMC: 9857982. DOI: 10.3390/foods12020360.

Starch Branching Enzyme 1 Is Important for Amylopectin Synthesis and Cyst Reactivation in Toxoplasma gondii.

Yang J, He Z, Chen C, Zhao J, Fang R Microbiol Spectr. 2022; 10(3):e0189121.

PMID: 35446124 PMC: 9241709. DOI: 10.1128/spectrum.01891-21.

A review of starch biosynthesis in cereal crops and its potential breeding applications in rice ( L.).

Li R, Zheng W, Jiang M, Zhang H PeerJ. 2022; 9:e12678.

PMID: 35036154 PMC: 8710062. DOI: 10.7717/peerj.12678.

References

Witt T, Doutch J, Gilbert E, Gilbert R . Relations between molecular, crystalline, and lamellar structures of amylopectin. Biomacromolecules. 2012; 13(12):4273-82. DOI: 10.1021/bm301586x. View

Yandeau-Nelson M, Laurens L, Shi Z, Xia H, Smith A, Guiltinan M . Starch-branching enzyme IIa is required for proper diurnal cycling of starch in leaves of maize. Plant Physiol. 2011; 156(2):479-90. PMC: 3177252. DOI: 10.1104/pp.111.174094. View

Hebelstrup K, Sagnelli D, Blennow A . The future of starch bioengineering: GM microorganisms or GM plants?. Front Plant Sci. 2015; 6:247. PMC: 4407504. DOI: 10.3389/fpls.2015.00247. View

Noguchi J, Chaen K, Vu N, Akasaka T, Shimada H, Nakashima T . Crystal structure of the branching enzyme I (BEI) from Oryza sativa L with implications for catalysis and substrate binding. Glycobiology. 2011; 21(8):1108-16. DOI: 10.1093/glycob/cwr049. View

Kuriki T, Takata H, Okada S, Imanaka T . Analysis of the active center of Bacillus stearothermophilus neopullulanase. J Bacteriol. 1991; 173(19):6147-52. PMC: 208363. DOI: 10.1128/jb.173.19.6147-6152.1991. View

Syahariza Z, Sar S, Hasjim J, Tizzotti M, Gilbert R . The importance of amylose and amylopectin fine structures for starch digestibility in cooked rice grains. Food Chem. 2012; 136(2):742-9. DOI: 10.1016/j.foodchem.2012.08.053. View

Pal K, Kumar S, Sharma S, Garg S, Alam M, Xu H . Crystal structure of full-length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal beta-sandwich in substrate specificity and enzymatic activity. J Biol Chem. 2010; 285(27):20897-903. PMC: 2898361. DOI: 10.1074/jbc.M110.121707. View

Wu A, Ral J, Morell M, Gilbert R . New perspectives on the role of α- and β-amylases in transient starch synthesis. PLoS One. 2014; 9(6):e100498. PMC: 4074105. DOI: 10.1371/journal.pone.0100498. View

Podkovyrov S, Burdette D, Zeikus J . Analysis of the catalytic center of cyclomaltodextrinase from Thermoanaerobacter ethanolicus 39E. FEBS Lett. 1993; 317(3):259-62. DOI: 10.1016/0014-5793(93)81288-b. View

10.

Nakamura Y . Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue. Plant Cell Physiol. 2002; 43(7):718-25. DOI: 10.1093/pcp/pcf091. View

11.

Palomo M, Kralj S, van der Maarel M, Dijkhuizen L . The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains. Appl Environ Microbiol. 2009; 75(5):1355-62. PMC: 2648161. DOI: 10.1128/AEM.02141-08. View

12.

Burton R, Bewley J, Smith A, Bhattacharyya M, Tatge H, Ring S . Starch branching enzymes belonging to distinct enzyme families are differentially expressed during pea embryo development. Plant J. 1995; 7(1):3-15. DOI: 10.1046/j.1365-313x.1995.07010003.x. View

13.

Gaj T, Gersbach C, Barbas 3rd C . ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering. Trends Biotechnol. 2013; 31(7):397-405. PMC: 3694601. DOI: 10.1016/j.tibtech.2013.04.004. View

14.

Santos C, Tonoli C, Trindade D, Betzel C, Takata H, Kuriki T . Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Proteins. 2010; 79(2):547-57. DOI: 10.1002/prot.22902. View

15.

Blauth S, Yao Y, Klucinec J, Shannon J, Thompson D, Guilitinan M . Identification of Mutator insertional mutants of starch-branching enzyme 2a in corn. Plant Physiol. 2001; 125(3):1396-405. PMC: 65618. DOI: 10.1104/pp.125.3.1396. View

16.

Kuriki T, Guan H, Sivak M, Preiss J . Analysis of the active center of branching enzyme II from maize endosperm. J Protein Chem. 1996; 15(3):305-13. DOI: 10.1007/BF01887119. View

17.

Nishi A, Nakamura Y, Tanaka N, Satoh H . Biochemical and genetic analysis of the effects of amylose-extender mutation in rice endosperm. Plant Physiol. 2001; 127(2):459-72. PMC: 125082. View

18.

Takata H, Takaha T, Okada S, Takagi M, Imanaka T . Cyclization reaction catalyzed by branching enzyme. J Bacteriol. 1996; 178(6):1600-6. PMC: 177844. DOI: 10.1128/jb.178.6.1600-1606.1996. View

19.

Keeling P, Myers A . Biochemistry and genetics of starch synthesis. Annu Rev Food Sci Technol. 2011; 1:271-303. DOI: 10.1146/annurev.food.102308.124214. View

20.

Klein C, Schulz G . Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution. J Mol Biol. 1991; 217(4):737-50. DOI: 10.1016/0022-2836(91)90530-j. View