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http://krishi.icar.gov.in/jspui/handle/123456789/44232
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Not Available | en_US |
dc.contributor.author | N H Mohan, M.Choudhury, L Ammayappan, Prajwalita Pathak, Sujay Chakraborty, R. Thomas,S.Debnath, Maitry Paul and D.K.Sarma | en_US |
dc.date.accessioned | 2020-12-30T04:02:32Z | - |
dc.date.available | 2020-12-30T04:02:32Z | - |
dc.date.issued | 2020-12-28 | - |
dc.identifier.citation | Mohan NH , M. Choudhury , L. Ammayappan , Prajwalita Pathak , Sujay Chakraborty , R. Thomas , S. Debnath , Maitry Paul & D. K. Sarma (2020).Characterization of Secondary Structure of Pig Hair Fiber Using Fourier-transform Infrared Spectroscopy. Journal of Natural Fibers, DOI: 10.1080/15440478.2020.1856272 | en_US |
dc.identifier.other | DOI: 10.1080/15440478.2020.1856272 | - |
dc.identifier.uri | http://krishi.icar.gov.in/jspui/handle/123456789/44232 | - |
dc.description | Not Available | en_US |
dc.description.abstract | Hair or bristle is one of the key by-products of humane slaughter of pigs. In the present study, Fourier-transform infrared (FTIR) spectroscopy was used for examining protein secondary structure of hair fier from diffrent breeds of pigs (Ghungroo, Ninag Megha, Hampshire, and Duroc). Prominent amide I (1635–1648 cm−1 ) and amide II (1517–1528 cm −1 ) bands could be observed in the spectra. Diffrences in presence/absence of certain FTIR bands between breeds suggests inflence of genetic background in the structure of hair fier. Deconvolution resolved secondary structure of protein in amide I region of spectra into corresponding α-helix (38.0 ± 2.9%), β-sheets (32.2 ± 2.0%), β-turns (19.4 ± 3.1%) and unorganized structural components (10.3 ± 2.5%). Heating of fiers from 80°C to 120°C resulted in changes in amide regions and α-helix to β-sheet ratio of amide I band. Further, correlations were calculated between area under the curve of various FTIR bands and tensile properties of the fier. Area of FTIR band at 1635 cm −1 was positively correlated with tenacity, initial modulus, extensibility, and work of rupture (r = 0.30 to 0.39). In nutshell, the study reveals subtle diffrences in secondary structure of hair with respect to breed or temperature treatment and suggests relation between FTIR spectral characteristics and tensile properties. | en_US |
dc.description.sponsorship | Indian Council of Agricultural Research | en_US |
dc.language.iso | English | en_US |
dc.publisher | Journal of Natural Fibers, Taylor and Francis | en_US |
dc.relation.ispartofseries | Not Available; | - |
dc.subject | pig hair, FTIR, protein structure | en_US |
dc.title | Characterization of Secondary Structure of Pig Hair Fiber Using Fourier-transform Infrared Spectroscopy | en_US |
dc.title.alternative | Not Available | en_US |
dc.type | Article | en_US |
dc.publication.projectcode | Not Available | en_US |
dc.publication.journalname | Journal of Natural Fibers | en_US |
dc.publication.volumeno | Not Available | en_US |
dc.publication.pagenumber | Not Available | en_US |
dc.publication.divisionUnit | Not Available | en_US |
dc.publication.sourceUrl | DOI: 10.1080/15440478.2020.1856272 | en_US |
dc.publication.authorAffiliation | ICAR::National Research Centre on Pig | en_US |
dc.ICARdataUseLicence | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf | en_US |
dc.publication.naasrating | 8.62 | en_US |
Appears in Collections: | AS-NRCP-Publication |
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