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Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure

Walnut protein is a kind of natural, high-quality plant protein resource. However, its high content of gluten, strong hydrophobicity and poor gelation ability have greatly limited its development and utilization in gel products. It was found in this experiment that ultrasonic power combined with tra...

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Autores principales: Liu, Yanlong, Lei, Yuqing, Kang, Xu, Ouyang, Hui, Li, Xiuting, Yu, Xiongwei, Gu, Qianhui, Li, Shugang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9957005/
https://www.ncbi.nlm.nih.gov/pubmed/36826261
http://dx.doi.org/10.3390/gels9020091
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author Liu, Yanlong
Lei, Yuqing
Kang, Xu
Ouyang, Hui
Li, Xiuting
Yu, Xiongwei
Gu, Qianhui
Li, Shugang
author_facet Liu, Yanlong
Lei, Yuqing
Kang, Xu
Ouyang, Hui
Li, Xiuting
Yu, Xiongwei
Gu, Qianhui
Li, Shugang
author_sort Liu, Yanlong
collection PubMed
description Walnut protein is a kind of natural, high-quality plant protein resource. However, its high content of gluten, strong hydrophobicity and poor gelation ability have greatly limited its development and utilization in gel products. It was found in this experiment that ultrasonic power combined with transglutaminase (TGase) had a significant effect on the gel properties of the walnut protein isolate (WNPI)-κ-carrageenan (KC) complex. The results showed that the gel strength of the WNPI-KC complex first increased and then decreased with the increase in ultrasonic power (0–400 W). WNPI-KC composite gel had the best texture properties, rheological properties, water-holding capacity (99.41 ± 0.76%), swelling ratio (2.31 ± 0.29%) and thermal stability (83.22 °C) following 200 W ultrasonic pretreatment. At this time, the gel network was more uniform and much denser, and the water molecules were more tightly bound. Further, 200 W ultrasonic pretreatment could promote the transformation of α-helices to β-folds in protein molecules, improve the fluorescence intensity, increase the content of free sulfhydryl groups and enhance the intermolecular forces. The experimental results could provide technical support for the development of walnut protein gel food.
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spelling pubmed-99570052023-02-25 Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure Liu, Yanlong Lei, Yuqing Kang, Xu Ouyang, Hui Li, Xiuting Yu, Xiongwei Gu, Qianhui Li, Shugang Gels Article Walnut protein is a kind of natural, high-quality plant protein resource. However, its high content of gluten, strong hydrophobicity and poor gelation ability have greatly limited its development and utilization in gel products. It was found in this experiment that ultrasonic power combined with transglutaminase (TGase) had a significant effect on the gel properties of the walnut protein isolate (WNPI)-κ-carrageenan (KC) complex. The results showed that the gel strength of the WNPI-KC complex first increased and then decreased with the increase in ultrasonic power (0–400 W). WNPI-KC composite gel had the best texture properties, rheological properties, water-holding capacity (99.41 ± 0.76%), swelling ratio (2.31 ± 0.29%) and thermal stability (83.22 °C) following 200 W ultrasonic pretreatment. At this time, the gel network was more uniform and much denser, and the water molecules were more tightly bound. Further, 200 W ultrasonic pretreatment could promote the transformation of α-helices to β-folds in protein molecules, improve the fluorescence intensity, increase the content of free sulfhydryl groups and enhance the intermolecular forces. The experimental results could provide technical support for the development of walnut protein gel food. MDPI 2023-01-20 /pmc/articles/PMC9957005/ /pubmed/36826261 http://dx.doi.org/10.3390/gels9020091 Text en © 2023 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
Liu, Yanlong
Lei, Yuqing
Kang, Xu
Ouyang, Hui
Li, Xiuting
Yu, Xiongwei
Gu, Qianhui
Li, Shugang
Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure
title Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure
title_full Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure
title_fullStr Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure
title_full_unstemmed Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure
title_short Walnut Protein Isolate-κ-Carrageenan Composite Gels Improved with Synergetic Ultrasound-Transglutaminase: Gelation Properties and Structure
title_sort walnut protein isolate-κ-carrageenan composite gels improved with synergetic ultrasound-transglutaminase: gelation properties and structure
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9957005/
https://www.ncbi.nlm.nih.gov/pubmed/36826261
http://dx.doi.org/10.3390/gels9020091
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