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Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles

This study was conducted to evaluate the proteolysis trends and change in meat quality during 10 days of cold storage in duck M. pectoralis major (PM) and M. iliotibialis (IL). Duck IL had a higher pH and greater degree of lightness but lower cooking loss than PM (p<0.05). During the 10-day cold...

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Autores principales: Cheng, Huilin, Song, Sumin, Park, Tae Sub, Kim, Gap-Don
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Food Science of Animal Resources 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8907789/
https://www.ncbi.nlm.nih.gov/pubmed/35310569
http://dx.doi.org/10.5851/kosfa.2022.e2
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author Cheng, Huilin
Song, Sumin
Park, Tae Sub
Kim, Gap-Don
author_facet Cheng, Huilin
Song, Sumin
Park, Tae Sub
Kim, Gap-Don
author_sort Cheng, Huilin
collection PubMed
description This study was conducted to evaluate the proteolysis trends and change in meat quality during 10 days of cold storage in duck M. pectoralis major (PM) and M. iliotibialis (IL). Duck IL had a higher pH and greater degree of lightness but lower cooking loss than PM (p<0.05). During the 10-day cold storage, the pH value of PM declined significantly (p<0.05), while the meat quality traits of IL were not affected by cold storage (p>0.05). In PM, the redness increased from day 1 to day 5, while cooking loss was lower on day 10 compared to day 5 (p<0.05). There were no significant differences in the activities of cathepsin B and proteasome 20S during cold storage (p>0.05). The activity of calpains declined gradually during 10 days of storage (p<0.05), and the activity of calpains in PM was higher than that in IL (p<0.05). A total of 5,155 peptides were detected and derived from 34 proteins of duck PM muscle, whereas 4,222 peptides derived from 32 proteins were detected from duck IL muscle. Duck PM muscle was composed only of fast type of muscle fiber, whereas IL muscle was composed of both slow and fast types. The proteins responsible for glycolysis or myofibrillar proteins were closely related to changes in meat color or water-holding capacity during cold storage. These results suggest that changes in meat quality characteristics during cold storage are closely related to protein degradation, which is also related to the distribution of muscle fiber types.
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spelling pubmed-89077892022-03-17 Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles Cheng, Huilin Song, Sumin Park, Tae Sub Kim, Gap-Don Food Sci Anim Resour Article This study was conducted to evaluate the proteolysis trends and change in meat quality during 10 days of cold storage in duck M. pectoralis major (PM) and M. iliotibialis (IL). Duck IL had a higher pH and greater degree of lightness but lower cooking loss than PM (p<0.05). During the 10-day cold storage, the pH value of PM declined significantly (p<0.05), while the meat quality traits of IL were not affected by cold storage (p>0.05). In PM, the redness increased from day 1 to day 5, while cooking loss was lower on day 10 compared to day 5 (p<0.05). There were no significant differences in the activities of cathepsin B and proteasome 20S during cold storage (p>0.05). The activity of calpains declined gradually during 10 days of storage (p<0.05), and the activity of calpains in PM was higher than that in IL (p<0.05). A total of 5,155 peptides were detected and derived from 34 proteins of duck PM muscle, whereas 4,222 peptides derived from 32 proteins were detected from duck IL muscle. Duck PM muscle was composed only of fast type of muscle fiber, whereas IL muscle was composed of both slow and fast types. The proteins responsible for glycolysis or myofibrillar proteins were closely related to changes in meat color or water-holding capacity during cold storage. These results suggest that changes in meat quality characteristics during cold storage are closely related to protein degradation, which is also related to the distribution of muscle fiber types. Korean Society for Food Science of Animal Resources 2022-03 2022-03-01 /pmc/articles/PMC8907789/ /pubmed/35310569 http://dx.doi.org/10.5851/kosfa.2022.e2 Text en © Korean Society for Food Science of Animal Resources https://creativecommons.org/licenses/by-nc/3.0/This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Article
Cheng, Huilin
Song, Sumin
Park, Tae Sub
Kim, Gap-Don
Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles
title Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles
title_full Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles
title_fullStr Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles
title_full_unstemmed Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles
title_short Comparison of Meat Quality Characteristics and Proteolysis Trends associated with Muscle Fiber Type Distribution between Duck Pectoralis Major and Iliotibialis Muscles
title_sort comparison of meat quality characteristics and proteolysis trends associated with muscle fiber type distribution between duck pectoralis major and iliotibialis muscles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8907789/
https://www.ncbi.nlm.nih.gov/pubmed/35310569
http://dx.doi.org/10.5851/kosfa.2022.e2
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