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Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis
In this paper, the effects of different modification orders of microbial transglutaminase (MTGase) and contents of pectin (0.1–0.5%, w/v) on the gelling and structural properties of fish gelatin (FG) and the modification mechanism were studied. The results showed that the addition of pectin could ov...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10453174/ https://www.ncbi.nlm.nih.gov/pubmed/37628026 http://dx.doi.org/10.3390/foods12163027 |
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author | Su, Kaiyuan Sun, Wanyi Li, Zhang Huang, Tao Lou, Qiaoming Zhan, Shengnan |
author_facet | Su, Kaiyuan Sun, Wanyi Li, Zhang Huang, Tao Lou, Qiaoming Zhan, Shengnan |
author_sort | Su, Kaiyuan |
collection | PubMed |
description | In this paper, the effects of different modification orders of microbial transglutaminase (MTGase) and contents of pectin (0.1–0.5%, w/v) on the gelling and structural properties of fish gelatin (FG) and the modification mechanism were studied. The results showed that the addition of pectin could overcome the phenomenon of high-MTGase-induced lower gelling strength of gelatin gels. At a low pectin content, the modification sequences had non-significant influence on the gelling properties of modified FG, but at a higher pectin content (0.5%, w/v), P(0.5%)-FG-TG had higher gel strength (751.99 ± 10.9 g) and hardness (14.91 ± 0.33 N) values than those of TG-FG-P(0.5%) (687.67 ± 20.98 g, 12.18 ± 0.45 N). Rheology analysis showed that the addition of pectin normally improved the gelation points and melting points of FG. The structural results showed that the fluorescence intensity of FG was decreased with the increase in pectin concentration. Fourier transform infrared spectroscopy analysis indicated that the MTGase and pectin complex modifications could influence the secondary structure of FG, but the influenced mechanisms were different. FG was firstly modified by MTGase, and then pectin (P-FG-TG) had the higher gelling and stability properties. |
format | Online Article Text |
id | pubmed-10453174 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104531742023-08-26 Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis Su, Kaiyuan Sun, Wanyi Li, Zhang Huang, Tao Lou, Qiaoming Zhan, Shengnan Foods Article In this paper, the effects of different modification orders of microbial transglutaminase (MTGase) and contents of pectin (0.1–0.5%, w/v) on the gelling and structural properties of fish gelatin (FG) and the modification mechanism were studied. The results showed that the addition of pectin could overcome the phenomenon of high-MTGase-induced lower gelling strength of gelatin gels. At a low pectin content, the modification sequences had non-significant influence on the gelling properties of modified FG, but at a higher pectin content (0.5%, w/v), P(0.5%)-FG-TG had higher gel strength (751.99 ± 10.9 g) and hardness (14.91 ± 0.33 N) values than those of TG-FG-P(0.5%) (687.67 ± 20.98 g, 12.18 ± 0.45 N). Rheology analysis showed that the addition of pectin normally improved the gelation points and melting points of FG. The structural results showed that the fluorescence intensity of FG was decreased with the increase in pectin concentration. Fourier transform infrared spectroscopy analysis indicated that the MTGase and pectin complex modifications could influence the secondary structure of FG, but the influenced mechanisms were different. FG was firstly modified by MTGase, and then pectin (P-FG-TG) had the higher gelling and stability properties. MDPI 2023-08-11 /pmc/articles/PMC10453174/ /pubmed/37628026 http://dx.doi.org/10.3390/foods12163027 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 Su, Kaiyuan Sun, Wanyi Li, Zhang Huang, Tao Lou, Qiaoming Zhan, Shengnan Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis |
title | Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis |
title_full | Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis |
title_fullStr | Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis |
title_full_unstemmed | Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis |
title_short | Complex Modification Orders Alleviate the Gelling Weakening Behavior of High Microbial Transglutaminase (MTGase)-Catalyzed Fish Gelatin: Gelling and Structural Analysis |
title_sort | complex modification orders alleviate the gelling weakening behavior of high microbial transglutaminase (mtgase)-catalyzed fish gelatin: gelling and structural analysis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10453174/ https://www.ncbi.nlm.nih.gov/pubmed/37628026 http://dx.doi.org/10.3390/foods12163027 |
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