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Structural and Functional Properties of Food Proteins

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Food Chemistry".

Deadline for manuscript submissions: closed (31 May 2024) | Viewed by 1491

Special Issue Editor


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Guest Editor
School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China
Interests: meat and aquatic products; plant proteins; protein physiochemistry; protein functionality; freezing
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Special Issue Information

Dear Colleagues,

The function of a molecules depends on their structure and that proteins in food can assemble into functional structures, those structures are dynamic and will respond to exterior factors during food processing, storage, and intake. The multifunctional properties (gelation, emulsification, water-binding, foaming, etc.) of proteins provide food with different textures, while the amino acid composition and digestibility largely determine the nutritional value of food proteins. Both the structure and function of food proteins can be modulated via physicochemical methods. The structure–function relationship of proteins has been widely studied in traditional foods, while recently there is growing interest in novel protein ingredients. Due to the complex interaction between proteins and the food matrix, the structure–function relationship of proteins derived from the model system can be quite different from real foods. This Special Issue of Molecules, entitled “Structural and Functional Properties of Food Proteins”, aims to collect original research focusing on the structure–function properties of food proteins. Review papers which discuss current understanding and point out future research directions are also welcome.

Prof. Dr. Yulong Bao
Guest Editor

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Keywords

  • protein structure
  • gelation
  • emulsification
  • water-holding
  • digestion
  • protein modification
  • food matrix

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Published Papers (1 paper)

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Research

17 pages, 6634 KiB  
Article
Purification, Characterization, cDNA Cloning, and Bioinformatic Analysis of Zinc-Binding Protein from Magallana hongkongensis
by Citing Chen, Wan Li, Jialong Gao, Wenhong Cao, Xiaoming Qin, Huina Zheng, Haisheng Lin and Zhongqin Chen
Molecules 2024, 29(4), 900; https://doi.org/10.3390/molecules29040900 - 18 Feb 2024
Viewed by 1184
Abstract
Oysters contain significant amounts of the zinc element, which may also be found in their proteins. In this study, a novel zinc-binding protein was purified from the mantle of the oyster Magallana hongkongensis using two kinds of gel filtration chromatograms. Sodium dodecyl sulfate–polyacrylamide [...] Read more.
Oysters contain significant amounts of the zinc element, which may also be found in their proteins. In this study, a novel zinc-binding protein was purified from the mantle of the oyster Magallana hongkongensis using two kinds of gel filtration chromatograms. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) showed that its molecular weight was approximately 36 kDa. The protein identified by the Q-Exactive mass spectrometer shared the highest sequence identity with carbonic anhydrase derived from Crassostrea gigas concerning amino acid sequence similarity. Based on homologous cloning and RACE PCR, the full-length cDNA of carbonic anhydrase from Magallana hongkongensis (designated as MhCA) was cloned and sequenced. The cDNA of MhCA encodes a 315-amino-acid protein with 89.74% homology to carbonic anhydrase derived from Crassostrea gigas. Molecular docking revealed that the two zinc ions primarily form coordination bonds with histidine residues in the MhCA protein. These results strongly suggest that MhCA is a novel zinc-binding protein in Magallana hongkongensis. Full article
(This article belongs to the Special Issue Structural and Functional Properties of Food Proteins)
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