Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/608261
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dc.date.accessioned2024-12-19T11:35:54Z-
dc.date.available2024-12-19T11:35:54Z-
dc.identifier.urihttp://hdl.handle.net/10603/608261-
dc.description.abstractComprehensive analysis of gelatin extracted from water buffalo hide, pig, sheep, newlinebroiler chicken and spent hen skins using different acid and/alkali pre-treatment newlinefollowed by thermo-hydrolysis was carried out. Highest (P lt 0.05) gelatin yield was newlineobtained from sheep skin (SSG, 9.55%) and water buffalo hide (BHG, 9.47%) relative newlineto chicken (CSG, 6.06%), pig (PSG, 5.98%) and spent hen (SHSG, 5.98%) skins, newlinerespectively. The SSG showed highest transmittance (%) among all the gelatin samples. newlineBuffalo hide presented the highest collagen solubility (75.76%), followed by chicken newline(68.95%), sheep (59.58%), spent hen (11.74%) and pig (5.23%) skin, respectively. The newlinePSG gels showed lower L*, a* and b* values and higher (P lt 0.05) viscosity relative to newlineother samples. The SSG had higher (P lt 0.05) gel strength, foaming capacity and newlinefoaming stability as compared to others. Fourier transform infrared (FTIR) spectroscopy newlineanalysis of gelatin exhibited the presence of amide-I peaks for all samples in the lower newlinefrequency range (1629.9-1647.26 cm-1), whereas, only SSG, BHG and PSG revealed newlineamide-II peaks at lower frequency range (1500.67-1523.82 cm-1) indicating NH newlinedeformation. Scanning electron microscopy analysis revealed that BHG gel had a newlineconsistent network of thicker strands and medium-sized holes whereas, PSG and SSG newlinegel showed a sheet-like appearance with no voids. The SDS-PAGE fractionation of newlineextracted gelatin powder followed by MALDI-TOF MS analysis has identified the newlinecollagen alpha 1 (I) chain as a predominant component responsible for gelatin stability newlineand detected unique species-specific peptides. Current study has demonstrated the newlinepotential of using water buffalo hide and sheep skin as an alternative to pig skin/bovine newlinehides or bones for industrial production of gelatin with superior quality attributes. newlineIn the second phase of experiment, the binary mixture samples were prepared by newlinespiking chicken meat patties (CMP) with 0.1, 0.5, 1.0 and 2.5% (w/w) of in-house derived newlinepig skin gelatin (PSG)/water buffalo hide gelatin (
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dc.languageEnglish
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dc.rightsuniversity
dc.titleQuantitative Identification Characterization And Validation Of Species Specific Animal Derived Gelatin By Conventional And Multiple Reaction Monitoring Mass Spectrometry Approaches
dc.title.alternative
dc.creator.researcherBIDYUT PRAVA MISHRA
dc.subject.keywordLife Sciences
dc.subject.keywordPlant and Animal Science
dc.subject.keywordVeterinary Sciences disease in animals
dc.description.note
dc.contributor.guideESWARA RAO .B, NAVEENA .B.M, NAGA MALLIKA .E, SRINIVASA RAO .T, NARENDRA NATH .D
dc.publisher.placeTirupati
dc.publisher.universitySri Venkateswara Veterinary University, Tirupati
dc.publisher.institutionLivestock Products Technology
dc.date.registered2020
dc.date.completed2023
dc.date.awarded2023
dc.format.dimensions
dc.format.accompanyingmaterialDVD
dc.source.universityUniversity
dc.type.degreePh.D.
Appears in Departments:Livestock Products Technology

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02-prelims pages.pdf877.53 kBAdobe PDFView/Open
03-content.pdf516.44 kBAdobe PDFView/Open
04-abstract.pdf308.2 kBAdobe PDFView/Open
05-chapter 1.pdf139.26 kBAdobe PDFView/Open
06-chapter 2.pdf487.52 kBAdobe PDFView/Open
07-chapter 3.pdf3.66 MBAdobe PDFView/Open
08-chapter 4.pdf5.44 MBAdobe PDFView/Open
09-chapter 5.pdf556.01 kBAdobe PDFView/Open
10-chapter 6.pdf537.96 kBAdobe PDFView/Open
11-literature.pdf432.24 kBAdobe PDFView/Open
80_recommendation.pdf289.63 kBAdobe PDFView/Open


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