Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

This study primarily explored the internal mechanism underlying the ultrasonication-induced release of antioxidant peptides. An oxhide gelatin solution was treated ultrasonically (power = 200, 300, and 400 W), followed by enzymatic hydrolysis and structural and morphological analysis. The results sh...

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Main Authors: Long He, Yongfang Gao, Xinyue Wang, Ling Han, Qunli Yu, Hongmei Shi, Rende Song
Format: Article
Language:English
Published: Elsevier 2021-10-01
Series:Ultrasonics Sonochemistry
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S1350417721002807
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author Long He
Yongfang Gao
Xinyue Wang
Ling Han
Qunli Yu
Hongmei Shi
Rende Song
author_facet Long He
Yongfang Gao
Xinyue Wang
Ling Han
Qunli Yu
Hongmei Shi
Rende Song
author_sort Long He
collection DOAJ
description This study primarily explored the internal mechanism underlying the ultrasonication-induced release of antioxidant peptides. An oxhide gelatin solution was treated ultrasonically (power = 200, 300, and 400 W), followed by enzymatic hydrolysis and structural and morphological analysis. The results showed that ultrasonication increased not only the degree of hydrolysis (DH) and protein recovery rate of the oxhide gelatin but also the ABTS radical scavenging, DPPH radical scavenging, ferrous chelating, and ferric reducing activities of its hydrolysate. The oxhide gelatin hydrolysate treated with 300-W ultrasonication had the maximum antioxidant activities. Ultrasonication inhibited hydrogen bond formation, reduced the crosslinking between collagen molecules, transformed part of the folded structure into a helical structure, and lowered the thermal stability of collagen molecules. The micromorphological analysis revealed that ultrasonication caused the gelatin surface to become loose and develop cracks, and as the power of the ultrasonication increased, the repetition interval distance (dÅ) also increased. Moreover, ultrasonication improved the solubilization, surface hydrophobicity, and interface characteristics and increased the content of basic and aromatic amino acids in the hydrolysate. In conclusion, ultrasonication modifies the protein structure, which increases the enzyme’s accessibility to the peptide bonds and further enhances antioxidant peptide release. These findings provide new insights into the application of ultrasonication in the release of antioxidant peptides.
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spelling doaj.art-1fb211cf635c4ba0b19c752049fd75cd2022-12-21T18:42:32ZengElsevierUltrasonics Sonochemistry1350-41772021-10-0178105738Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structureLong He0Yongfang Gao1Xinyue Wang2Ling Han3Qunli Yu4Hongmei Shi5Rende Song6College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, ChinaLaboratory of Agricultural & Food Biomechanics, Institute of Biophysics, College of Science, Northwest A & F University, Yangling, Shaanxi 712100, ChinaCollege of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, ChinaCollege of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, ChinaCollege of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, China; Corresponding author.The Institute of Animal Science and Veterinary, Hezuo 747000, ChinaThe Qinghai Work Station of Animal and Veterinary Sciences, Yushu 815000, ChinaThis study primarily explored the internal mechanism underlying the ultrasonication-induced release of antioxidant peptides. An oxhide gelatin solution was treated ultrasonically (power = 200, 300, and 400 W), followed by enzymatic hydrolysis and structural and morphological analysis. The results showed that ultrasonication increased not only the degree of hydrolysis (DH) and protein recovery rate of the oxhide gelatin but also the ABTS radical scavenging, DPPH radical scavenging, ferrous chelating, and ferric reducing activities of its hydrolysate. The oxhide gelatin hydrolysate treated with 300-W ultrasonication had the maximum antioxidant activities. Ultrasonication inhibited hydrogen bond formation, reduced the crosslinking between collagen molecules, transformed part of the folded structure into a helical structure, and lowered the thermal stability of collagen molecules. The micromorphological analysis revealed that ultrasonication caused the gelatin surface to become loose and develop cracks, and as the power of the ultrasonication increased, the repetition interval distance (dÅ) also increased. Moreover, ultrasonication improved the solubilization, surface hydrophobicity, and interface characteristics and increased the content of basic and aromatic amino acids in the hydrolysate. In conclusion, ultrasonication modifies the protein structure, which increases the enzyme’s accessibility to the peptide bonds and further enhances antioxidant peptide release. These findings provide new insights into the application of ultrasonication in the release of antioxidant peptides.http://www.sciencedirect.com/science/article/pii/S1350417721002807UltrasonicationOxhide gelatinAntioxidant peptidesMicrostructure
spellingShingle Long He
Yongfang Gao
Xinyue Wang
Ling Han
Qunli Yu
Hongmei Shi
Rende Song
Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
Ultrasonics Sonochemistry
Ultrasonication
Oxhide gelatin
Antioxidant peptides
Microstructure
title Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
title_full Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
title_fullStr Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
title_full_unstemmed Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
title_short Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
title_sort ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure
topic Ultrasonication
Oxhide gelatin
Antioxidant peptides
Microstructure
url http://www.sciencedirect.com/science/article/pii/S1350417721002807
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