Gelling mechanism of RG-I enriched citrus pectin: Role of arabinose side-chains in cation- and acid-induced gelation

Authors
Zheng, Jiaqi
Chen, Jianle
Zhang, Hua
Wu, Dongmei
Ye, Xingqian
Linardt, Robert J.
Chen, Shiguo
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2020-04-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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Full Citation
Gelling mechanism of RG-I enriched citrus pectin: Role of arabinose side-chains in cation- and acid-induced gelation, J. Zheng, J. Chen, H. Zhang, D. Wu, X. Ye, R. J. Linhardt, S. Chen, Food Hydrocolloids, 101, 105536, 2020.
Abstract
RG-I enriched pectin is present in fruit and vegetable containing products. However, it is removed by the hot acid treatment during commercial pectin production to improve gelling properties and to afford a more uniform pectin quality. Recently, an awareness of the health benefits of RG-I enriched pectin has caused technologists to rethink its utilization by the food industry, especially as a novel healthy gelling agent. Unique RG-I enriched pectin with abundant arabinan side-chains was extracted from citrus membrane by sequential mild acidic and alkaline treatment. Arabinose was then removed by enzymatic treatment to investigate the impact of arabinose side-chains on gelation. The properties of RG-I enriched pectin gels, prepared using cations or acid, showed it could form gels under conditions required for both low and high methoxyl pectin as a result of its highly branched structure. In cation-induced gelation, the HG region forms egg-box junction zones with divalent cations and the side-chains of the RG-I region stabilizes the network structure through entanglements. In acid-induced gelation, low pH promotes formation of hydrogen bonding and hydrophobic interactions within the HG region and the side-chains create a tighter conformation, eventually allowing for stronger interactions between the pectin chains.
Description
Food Hydrocolloids, 101, 105536
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Food Hydrocolloids
https://harc.rpi.edu/
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https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.foodhyd.2019.105536