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Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain

Different techniques have been applied in feed processing to improve ruminal degradation and nutrient utilization in ruminant. There are limited studies investigating how moist heating process impacts barley protein utilization and internal molecular structures. The objectives of this study were to...

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Detalles Bibliográficos
Autores principales: Feng, Xin, Sun, Baoli, Zhang, Huihua, Yu, Peiqiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7274425/
https://www.ncbi.nlm.nih.gov/pubmed/32502162
http://dx.doi.org/10.1371/journal.pone.0234126
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author Feng, Xin
Sun, Baoli
Zhang, Huihua
Yu, Peiqiang
author_facet Feng, Xin
Sun, Baoli
Zhang, Huihua
Yu, Peiqiang
author_sort Feng, Xin
collection PubMed
description Different techniques have been applied in feed processing to improve ruminal degradation and nutrient utilization in ruminant. There are limited studies investigating how moist heating process impacts barley protein utilization and internal molecular structures. The objectives of this study were to investigate: 1) how moist heating affects barley protein chemical profiles and Cornell Net Carbohydrate and Protein System (CNCPS) subfractions, in situ rumen degradation parameters, and predicted intestinal protein supply and feed milk value; 2) how moist heating affects protein molecular spectral features; and 3) the relationship between protein molecular structure spectral features and protein chemical profiles and metabolic characteristics. The barley variety CDC cowboy samples collected from the research farm during two consecutive years were used. Half of each sample was kept as raw and the other half underwent moist heating. The advanced molecular spectroscopy (attenuated total reflectance-fourier transform infrared, ATR-FTIR) was used to detect the barley protein molecular structure spectral features. It was found that moist heating decreased the fractions of soluble protein and increased the moderately degradable protein and ingestible protein fractions. This further resulted in the changes of in situ rumen degradation parameters and intestinal protein digestion characteristics. The protein molecular structure spectral features detected by using ATR-FTIR spectroscopy can be used as potential predictors for protein related chemical and metabolic parameters.
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spelling pubmed-72744252020-06-09 Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain Feng, Xin Sun, Baoli Zhang, Huihua Yu, Peiqiang PLoS One Research Article Different techniques have been applied in feed processing to improve ruminal degradation and nutrient utilization in ruminant. There are limited studies investigating how moist heating process impacts barley protein utilization and internal molecular structures. The objectives of this study were to investigate: 1) how moist heating affects barley protein chemical profiles and Cornell Net Carbohydrate and Protein System (CNCPS) subfractions, in situ rumen degradation parameters, and predicted intestinal protein supply and feed milk value; 2) how moist heating affects protein molecular spectral features; and 3) the relationship between protein molecular structure spectral features and protein chemical profiles and metabolic characteristics. The barley variety CDC cowboy samples collected from the research farm during two consecutive years were used. Half of each sample was kept as raw and the other half underwent moist heating. The advanced molecular spectroscopy (attenuated total reflectance-fourier transform infrared, ATR-FTIR) was used to detect the barley protein molecular structure spectral features. It was found that moist heating decreased the fractions of soluble protein and increased the moderately degradable protein and ingestible protein fractions. This further resulted in the changes of in situ rumen degradation parameters and intestinal protein digestion characteristics. The protein molecular structure spectral features detected by using ATR-FTIR spectroscopy can be used as potential predictors for protein related chemical and metabolic parameters. Public Library of Science 2020-06-05 /pmc/articles/PMC7274425/ /pubmed/32502162 http://dx.doi.org/10.1371/journal.pone.0234126 Text en © 2020 Feng et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Feng, Xin
Sun, Baoli
Zhang, Huihua
Yu, Peiqiang
Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
title Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
title_full Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
title_fullStr Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
title_full_unstemmed Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
title_short Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
title_sort using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7274425/
https://www.ncbi.nlm.nih.gov/pubmed/32502162
http://dx.doi.org/10.1371/journal.pone.0234126
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