Understanding CGTase action through the relationship between starch structure and cyclodextrin formation

The action of the enzyme CGTase on corn and potato starch was studied to understand the influence of starch structure and cyclodextrin (CD) production. Native and hydrolysed materials were analysed using multiple characterisation methods enabling coverage over more than six orders of magnitude in length-scale. The production of CD was greater for corn than potato but the relative abundance between different CD molecules was conserved. Structural differences were observed for all length scales investigated as a result of hydrolysis but to different extents between the starches. These observations were explained by differing modes of enzymatic attack between starch varieties. In corn, surface pores facilitated action of CGTase with hydrolysis generating limited changes in crystallinity and surface granule order. Hydrolysis of potato starch resulted in erosion at the granule surface, increase in surface order and overall crystallinity. Hydrolysis had minimal effect on the gelatinisation behaviour of both starches. Changes in the small-angle scattering due to CGTase confirmed the different mode of action of the enzyme between the two starches. Following hydrolysis, these changes in corn were consistent with preferential attack of the amorphous lamellae, while in potato, preferential hydrolysis of amorphous growth rings was indicated. These findings provide new insight into this industrially relevant enzyme and will assist in the optimisation of CGTase-based processing conditions for the development of novel products.

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Bibliographic Details
Main Authors: Benavent Gil, Yaiza, Rosell, Cristina M., Gilbert, Elliot P.
Other Authors: Ministerio de Ciencia, Innovación y Universidades (España)
Format: artículo biblioteca
Language:English
Published: Elsevier 2020-09-12
Subjects:CGTase, Cyclodextrin, Scattering, Structure, Corn, Potato,
Online Access:http://hdl.handle.net/10261/219607
http://dx.doi.org/10.13039/501100000780
http://dx.doi.org/10.13039/501100003359
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spelling dig-iata-es-10261-2196072021-09-12T04:31:08Z Understanding CGTase action through the relationship between starch structure and cyclodextrin formation Benavent Gil, Yaiza Rosell, Cristina M. Gilbert, Elliot P. Ministerio de Ciencia, Innovación y Universidades (España) European Commission Generalitat Valenciana CGTase Cyclodextrin Scattering Structure Corn Potato The action of the enzyme CGTase on corn and potato starch was studied to understand the influence of starch structure and cyclodextrin (CD) production. Native and hydrolysed materials were analysed using multiple characterisation methods enabling coverage over more than six orders of magnitude in length-scale. The production of CD was greater for corn than potato but the relative abundance between different CD molecules was conserved. Structural differences were observed for all length scales investigated as a result of hydrolysis but to different extents between the starches. These observations were explained by differing modes of enzymatic attack between starch varieties. In corn, surface pores facilitated action of CGTase with hydrolysis generating limited changes in crystallinity and surface granule order. Hydrolysis of potato starch resulted in erosion at the granule surface, increase in surface order and overall crystallinity. Hydrolysis had minimal effect on the gelatinisation behaviour of both starches. Changes in the small-angle scattering due to CGTase confirmed the different mode of action of the enzyme between the two starches. Following hydrolysis, these changes in corn were consistent with preferential attack of the amorphous lamellae, while in potato, preferential hydrolysis of amorphous growth rings was indicated. These findings provide new insight into this industrially relevant enzyme and will assist in the optimisation of CGTase-based processing conditions for the development of novel products. Authors acknowledge the financial support of the Spanish Ministry of Science, Innovation and Universities (Project RTI2018-095919-B-C21) and the European Regional Development Fund (FEDER) and Generalitat Valenciana (Project Prometeo 2017/189). Peer reviewed 2020-09-15T04:47:32Z 2020-09-15T04:47:32Z 2020-09-12 artículo http://purl.org/coar/resource_type/c_6501 Food Hydrocolloids 112: 106316 (2021) 0268-005X http://hdl.handle.net/10261/219607 10.1016/j.foodhyd.2020.106316 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100003359 en #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-095919-B-C21 Postprint https://doi.org/10.1016/j.foodhyd.2020.106316 Sí open Elsevier
institution IATA ES
collection DSpace
country España
countrycode ES
component Bibliográfico
access En linea
databasecode dig-iata-es
tag biblioteca
region Europa del Sur
libraryname Biblioteca del IATA España
language English
topic CGTase
Cyclodextrin
Scattering
Structure
Corn
Potato
CGTase
Cyclodextrin
Scattering
Structure
Corn
Potato
spellingShingle CGTase
Cyclodextrin
Scattering
Structure
Corn
Potato
CGTase
Cyclodextrin
Scattering
Structure
Corn
Potato
Benavent Gil, Yaiza
Rosell, Cristina M.
Gilbert, Elliot P.
Understanding CGTase action through the relationship between starch structure and cyclodextrin formation
description The action of the enzyme CGTase on corn and potato starch was studied to understand the influence of starch structure and cyclodextrin (CD) production. Native and hydrolysed materials were analysed using multiple characterisation methods enabling coverage over more than six orders of magnitude in length-scale. The production of CD was greater for corn than potato but the relative abundance between different CD molecules was conserved. Structural differences were observed for all length scales investigated as a result of hydrolysis but to different extents between the starches. These observations were explained by differing modes of enzymatic attack between starch varieties. In corn, surface pores facilitated action of CGTase with hydrolysis generating limited changes in crystallinity and surface granule order. Hydrolysis of potato starch resulted in erosion at the granule surface, increase in surface order and overall crystallinity. Hydrolysis had minimal effect on the gelatinisation behaviour of both starches. Changes in the small-angle scattering due to CGTase confirmed the different mode of action of the enzyme between the two starches. Following hydrolysis, these changes in corn were consistent with preferential attack of the amorphous lamellae, while in potato, preferential hydrolysis of amorphous growth rings was indicated. These findings provide new insight into this industrially relevant enzyme and will assist in the optimisation of CGTase-based processing conditions for the development of novel products.
author2 Ministerio de Ciencia, Innovación y Universidades (España)
author_facet Ministerio de Ciencia, Innovación y Universidades (España)
Benavent Gil, Yaiza
Rosell, Cristina M.
Gilbert, Elliot P.
format artículo
topic_facet CGTase
Cyclodextrin
Scattering
Structure
Corn
Potato
author Benavent Gil, Yaiza
Rosell, Cristina M.
Gilbert, Elliot P.
author_sort Benavent Gil, Yaiza
title Understanding CGTase action through the relationship between starch structure and cyclodextrin formation
title_short Understanding CGTase action through the relationship between starch structure and cyclodextrin formation
title_full Understanding CGTase action through the relationship between starch structure and cyclodextrin formation
title_fullStr Understanding CGTase action through the relationship between starch structure and cyclodextrin formation
title_full_unstemmed Understanding CGTase action through the relationship between starch structure and cyclodextrin formation
title_sort understanding cgtase action through the relationship between starch structure and cyclodextrin formation
publisher Elsevier
publishDate 2020-09-12
url http://hdl.handle.net/10261/219607
http://dx.doi.org/10.13039/501100000780
http://dx.doi.org/10.13039/501100003359
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AT rosellcristinam understandingcgtaseactionthroughtherelationshipbetweenstarchstructureandcyclodextrinformation
AT gilbertelliotp understandingcgtaseactionthroughtherelationshipbetweenstarchstructureandcyclodextrinformation
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