{"title":"驼皮漂白和脱脂处理对提取明胶的颜色、结构和界面性能的影响","authors":"Samson Olumide Fawale , Tholkappiyan Ramachandran , Hamed Fathalla , Sajid Maqsood","doi":"10.1016/j.foostr.2022.100275","DOIUrl":null,"url":null,"abstract":"<div><p>The effect of defatting and bleaching of camel skin on gel-forming, structural, and interfacial properties of extracted gelatin was studied. Gelatin defatted for 6 h and bleached for 48 h (48BD-6 h) gave the highest yield (28.44%) while gelatin bleached for 24 h (24 BC) gave the highest gel strength (423.3 g). Electrophoretic analysis showed that all gelatin samples had α-chains as the predominant protein type. Fourier transformation infrared (FTIR) spectroscopy showed that all gelatin samples possessed major peaks in the amide region with reduced peak intensity recorded in defatted and bleached samples because of the loss of the triple helix state of the gelatin. X-ray diffraction analysis indicated that all the gelatin samples are basically amorphous with both weak and sharp peaks observed around 7° and broad peaks at ~19–22°. Microstructural analysis revealed highly cross-linked network with less voids in all the gelatin samples which correlated with high gel strength recorded. Colour of the gelatin powder samples were significantly improved by bleaching with an increase in the <em>L</em><sup>∗</sup>-value and decrease in the <em>a</em><sup>∗</sup>-value. These results indicates that with bleaching, gelatin molecules were oxidized, resulting in the production of gelatin cross-links, giving gelatin an improved gel strength, colour, and functionality.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"33 ","pages":"Article 100275"},"PeriodicalIF":5.6000,"publicationDate":"2022-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"Effect of bleaching and defatting treatment of camel skin on the color, structural and interfacial properties of extracted gelatin\",\"authors\":\"Samson Olumide Fawale , Tholkappiyan Ramachandran , Hamed Fathalla , Sajid Maqsood\",\"doi\":\"10.1016/j.foostr.2022.100275\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The effect of defatting and bleaching of camel skin on gel-forming, structural, and interfacial properties of extracted gelatin was studied. Gelatin defatted for 6 h and bleached for 48 h (48BD-6 h) gave the highest yield (28.44%) while gelatin bleached for 24 h (24 BC) gave the highest gel strength (423.3 g). Electrophoretic analysis showed that all gelatin samples had α-chains as the predominant protein type. Fourier transformation infrared (FTIR) spectroscopy showed that all gelatin samples possessed major peaks in the amide region with reduced peak intensity recorded in defatted and bleached samples because of the loss of the triple helix state of the gelatin. X-ray diffraction analysis indicated that all the gelatin samples are basically amorphous with both weak and sharp peaks observed around 7° and broad peaks at ~19–22°. Microstructural analysis revealed highly cross-linked network with less voids in all the gelatin samples which correlated with high gel strength recorded. Colour of the gelatin powder samples were significantly improved by bleaching with an increase in the <em>L</em><sup>∗</sup>-value and decrease in the <em>a</em><sup>∗</sup>-value. These results indicates that with bleaching, gelatin molecules were oxidized, resulting in the production of gelatin cross-links, giving gelatin an improved gel strength, colour, and functionality.</p></div>\",\"PeriodicalId\":48640,\"journal\":{\"name\":\"Food Structure-Netherlands\",\"volume\":\"33 \",\"pages\":\"Article 100275\"},\"PeriodicalIF\":5.6000,\"publicationDate\":\"2022-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Structure-Netherlands\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2213329122000259\",\"RegionNum\":3,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Structure-Netherlands","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2213329122000259","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Effect of bleaching and defatting treatment of camel skin on the color, structural and interfacial properties of extracted gelatin
The effect of defatting and bleaching of camel skin on gel-forming, structural, and interfacial properties of extracted gelatin was studied. Gelatin defatted for 6 h and bleached for 48 h (48BD-6 h) gave the highest yield (28.44%) while gelatin bleached for 24 h (24 BC) gave the highest gel strength (423.3 g). Electrophoretic analysis showed that all gelatin samples had α-chains as the predominant protein type. Fourier transformation infrared (FTIR) spectroscopy showed that all gelatin samples possessed major peaks in the amide region with reduced peak intensity recorded in defatted and bleached samples because of the loss of the triple helix state of the gelatin. X-ray diffraction analysis indicated that all the gelatin samples are basically amorphous with both weak and sharp peaks observed around 7° and broad peaks at ~19–22°. Microstructural analysis revealed highly cross-linked network with less voids in all the gelatin samples which correlated with high gel strength recorded. Colour of the gelatin powder samples were significantly improved by bleaching with an increase in the L∗-value and decrease in the a∗-value. These results indicates that with bleaching, gelatin molecules were oxidized, resulting in the production of gelatin cross-links, giving gelatin an improved gel strength, colour, and functionality.
期刊介绍：
Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.
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