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Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim

Alternative protein sources for the human diet may help overcome the growing food pressure. Plants with abundant resources and high protein content are potential sources. In this article, graded proteins and isolated proteins from Corylus mandshurica Maxim kernels were extracted by the Osborne proce...

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Autores principales: Hou, Yanli, Ding, Jie, Guo, Qingqi, Zhang, Na
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10489673/
https://www.ncbi.nlm.nih.gov/pubmed/37687184
http://dx.doi.org/10.3390/molecules28176355
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author Hou, Yanli
Ding, Jie
Guo, Qingqi
Zhang, Na
author_facet Hou, Yanli
Ding, Jie
Guo, Qingqi
Zhang, Na
author_sort Hou, Yanli
collection PubMed
description Alternative protein sources for the human diet may help overcome the growing food pressure. Plants with abundant resources and high protein content are potential sources. In this article, graded proteins and isolated proteins from Corylus mandshurica Maxim kernels were extracted by the Osborne procedure and the alkali-solution and acid-isolation method, respectively, and the contents of the five proteins, and the differences in nutritional value and structural properties of the main proteins, were investigated. Amino acid analysis revealed that the total essential amino acids in the five proteins ranged from 249.58 to 324.52 mg/g. The essential amino acid profiles in the proteins were similar to those of FAO/WHO except for the alcohol-soluble protein. The essential amino acid indices ranged from 58.59 to 72.19 and the biological values ranged from 52.16 to 66.99, and the highest nutritional indices were found for the isolate and water-soluble protein, which were 41.68 and 55.78, respectively. The molecular weight pattern distribution of the protein isolates of the Corylus mandshurica Maxim kernel was more similar to that of the water-soluble proteins by SDS–PAGE. The β-sheet and α-helix were the main secondary structures in the two protein fractions. The fluorescence spectra showed that the maximum fluorescence intensity of the two proteins and their λmax were also somewhat different. From the perspective of microscopic morphology, the two proteins are mainly compact and irregular lamellar structures, but the surface of the water-soluble protein is more flat and regular. Both proteins have good solubility, and the water-soluble protein has higher solubility. In general, the protein isolates of the Corylus mandshurica Maxim kernel and the water-soluble protein showed their potential as plant protein resources.
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spelling pubmed-104896732023-09-09 Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim Hou, Yanli Ding, Jie Guo, Qingqi Zhang, Na Molecules Article Alternative protein sources for the human diet may help overcome the growing food pressure. Plants with abundant resources and high protein content are potential sources. In this article, graded proteins and isolated proteins from Corylus mandshurica Maxim kernels were extracted by the Osborne procedure and the alkali-solution and acid-isolation method, respectively, and the contents of the five proteins, and the differences in nutritional value and structural properties of the main proteins, were investigated. Amino acid analysis revealed that the total essential amino acids in the five proteins ranged from 249.58 to 324.52 mg/g. The essential amino acid profiles in the proteins were similar to those of FAO/WHO except for the alcohol-soluble protein. The essential amino acid indices ranged from 58.59 to 72.19 and the biological values ranged from 52.16 to 66.99, and the highest nutritional indices were found for the isolate and water-soluble protein, which were 41.68 and 55.78, respectively. The molecular weight pattern distribution of the protein isolates of the Corylus mandshurica Maxim kernel was more similar to that of the water-soluble proteins by SDS–PAGE. The β-sheet and α-helix were the main secondary structures in the two protein fractions. The fluorescence spectra showed that the maximum fluorescence intensity of the two proteins and their λmax were also somewhat different. From the perspective of microscopic morphology, the two proteins are mainly compact and irregular lamellar structures, but the surface of the water-soluble protein is more flat and regular. Both proteins have good solubility, and the water-soluble protein has higher solubility. In general, the protein isolates of the Corylus mandshurica Maxim kernel and the water-soluble protein showed their potential as plant protein resources. MDPI 2023-08-30 /pmc/articles/PMC10489673/ /pubmed/37687184 http://dx.doi.org/10.3390/molecules28176355 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
Hou, Yanli
Ding, Jie
Guo, Qingqi
Zhang, Na
Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim
title Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim
title_full Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim
title_fullStr Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim
title_full_unstemmed Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim
title_short Nutritional Value and Structure Characterization of Protein Components of Corylus mandshurica Maxim
title_sort nutritional value and structure characterization of protein components of corylus mandshurica maxim
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10489673/
https://www.ncbi.nlm.nih.gov/pubmed/37687184
http://dx.doi.org/10.3390/molecules28176355
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