Cargando…
Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility
Nonenzymatic browning (NEB) reactions often affect the nutritional quality and safety properties of amorphous food solids. Developing a proper approach to control the NEB reaction has been of particular interest in the food industry. An NEB reaction in an amorphous maltose/Whey protein isolates (WPI...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9324457/ https://www.ncbi.nlm.nih.gov/pubmed/35885371 http://dx.doi.org/10.3390/foods11142128 |
_version_ | 1784756811543347200 |
---|---|
author | Wu, Yaowen Ye, Haoxuan Fan, Fanghui |
author_facet | Wu, Yaowen Ye, Haoxuan Fan, Fanghui |
author_sort | Wu, Yaowen |
collection | PubMed |
description | Nonenzymatic browning (NEB) reactions often affect the nutritional quality and safety properties of amorphous food solids. Developing a proper approach to control the NEB reaction has been of particular interest in the food industry. An NEB reaction in an amorphous maltose/Whey protein isolates (WPI) matrix containing L-lysine and D-xylose as reactants were studied at ambient temperatures a(w) ≤ 0.44 and 45~65 °C. The results indicated that the presence of NEB reactants barely disturbed the water sorption behavior of the matrix. The Guggenheim–Anderson–de Boer (GAB) constants and Q(st) values of the studied samples were affected by storage conditions as the migration of sorbed water among monolayers occurred. The rate of color changes and 5-hydoxymethylfurfural (5-HMF) accumulation on the matrix were accelerated at high ambient temperatures a(w), reflecting the extent of NEB reaction increases. Since the strength concept (S) could give a measure of molecular mobility, the extent of the NEB reaction was governed by the molecular mobility of the matrix as the activation energy (E(a)) of 5-HMF production minimized at solids with high S values. We found that the S concept had a considerable potential usage in controlling the NEB reaction on amorphous sugar–protein solids. This data set has practical significance in the comprehensive understanding of manipulating the diffusion-limited chemical reactions on low-moisture food solids. |
format | Online Article Text |
id | pubmed-9324457 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93244572022-07-27 Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility Wu, Yaowen Ye, Haoxuan Fan, Fanghui Foods Article Nonenzymatic browning (NEB) reactions often affect the nutritional quality and safety properties of amorphous food solids. Developing a proper approach to control the NEB reaction has been of particular interest in the food industry. An NEB reaction in an amorphous maltose/Whey protein isolates (WPI) matrix containing L-lysine and D-xylose as reactants were studied at ambient temperatures a(w) ≤ 0.44 and 45~65 °C. The results indicated that the presence of NEB reactants barely disturbed the water sorption behavior of the matrix. The Guggenheim–Anderson–de Boer (GAB) constants and Q(st) values of the studied samples were affected by storage conditions as the migration of sorbed water among monolayers occurred. The rate of color changes and 5-hydoxymethylfurfural (5-HMF) accumulation on the matrix were accelerated at high ambient temperatures a(w), reflecting the extent of NEB reaction increases. Since the strength concept (S) could give a measure of molecular mobility, the extent of the NEB reaction was governed by the molecular mobility of the matrix as the activation energy (E(a)) of 5-HMF production minimized at solids with high S values. We found that the S concept had a considerable potential usage in controlling the NEB reaction on amorphous sugar–protein solids. This data set has practical significance in the comprehensive understanding of manipulating the diffusion-limited chemical reactions on low-moisture food solids. MDPI 2022-07-18 /pmc/articles/PMC9324457/ /pubmed/35885371 http://dx.doi.org/10.3390/foods11142128 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wu, Yaowen Ye, Haoxuan Fan, Fanghui Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility |
title | Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility |
title_full | Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility |
title_fullStr | Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility |
title_full_unstemmed | Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility |
title_short | Nonenzymatic Browning of Amorphous Maltose/Whey Protein Isolates Matrix: Effects of Water Sorption and Molecular Mobility |
title_sort | nonenzymatic browning of amorphous maltose/whey protein isolates matrix: effects of water sorption and molecular mobility |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9324457/ https://www.ncbi.nlm.nih.gov/pubmed/35885371 http://dx.doi.org/10.3390/foods11142128 |
work_keys_str_mv | AT wuyaowen nonenzymaticbrowningofamorphousmaltosewheyproteinisolatesmatrixeffectsofwatersorptionandmolecularmobility AT yehaoxuan nonenzymaticbrowningofamorphousmaltosewheyproteinisolatesmatrixeffectsofwatersorptionandmolecularmobility AT fanfanghui nonenzymaticbrowningofamorphousmaltosewheyproteinisolatesmatrixeffectsofwatersorptionandmolecularmobility |