Influence of Cross‐Linking by Microbial Transglutaminase on Physicochemical Properties of Eggshell Membrane Collagen.
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| Title: | Influence of Cross‐Linking by Microbial Transglutaminase on Physicochemical Properties of Eggshell Membrane Collagen. |
|---|---|
| Authors: | Kazemi Kheirabadi, Elahe1 (AUTHOR), Kheirandish, Poorandokht1 (AUTHOR), Razavi, Seyed Hadi1 (AUTHOR) srazavi@ut.ac.ir, Golmakani, Mohammad-Taghi2 (AUTHOR) golmakani@shirazu.ac.ir, Hebishy, Essam (AUTHOR) ehebishy+eic@wiley.com |
| Source: | Journal of Food Processing & Preservation. 6/28/2025, Vol. 2025, p1-9. 9p. |
| Subjects: | Differential scanning calorimetry, Amino group, Viscosity solutions, Scanning electron microscopy, Collagen |
| Abstract: | Collagen from eggshell membrane (EM) was stabilized via a cross‐linking procedure using microbial transglutaminase as an alternative, nontoxic cross‐linking reagent for its low stability and low mechanical strength. The physicochemical features of collagen solutions (5 mg/mL), which were cross‐linked by different concentrations of MTG (30, 40, 50, 60, and 70 U/g collagen), were examined. The SDS‐PAGE, differential scanning calorimetry (DSC), residual amino group content, scanning electron microscopy (SEM), and viscosity of solutions were evaluated. The results revealed that applying higher concentrations of MTG in cross‐linked collagen solutions leads to an increase of about 32°C–39°C in denaturation temperatures (Td) and a 75.76% decrease in residual amino group content. The simultaneous effect of different temperatures and concentrations of MTG on viscosity illustrated an improvement of approximately 30 Pa·s in the viscosity of cross‐linked collagen at 50°C. The enzymatically cross‐linked porous structures displayed finer microstructure with interlinked micron‐sized pores, exhibiting a 74% reduction in size compared to the uncross‐linked collagen. These results suggest that combining MTG and EM as sources of collagen represents an innovative potential route for the safe cross‐linking of collagen‐based matrices. This innovation could have practical applications in reducing waste EM, which is a by‐product of egg breaking in industrial and domestic settings, and utilize them to produce firmness and stabilize collagen. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of Food Processing & Preservation is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Header | DbId: egs DbLabel: Engineering Source An: 186251943 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Influence of Cross‐Linking by Microbial Transglutaminase on Physicochemical Properties of Eggshell Membrane Collagen. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Kazemi+Kheirabadi%2C+Elahe%22">Kazemi Kheirabadi, Elahe</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Kheirandish%2C+Poorandokht%22">Kheirandish, Poorandokht</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Razavi%2C+Seyed+Hadi%22">Razavi, Seyed Hadi</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> srazavi@ut.ac.ir</i><br /><searchLink fieldCode="AR" term="%22Golmakani%2C+Mohammad-Taghi%22">Golmakani, Mohammad-Taghi</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> golmakani@shirazu.ac.ir</i><br /><searchLink fieldCode="AR" term="%22Hebishy%2C+Essam%22">Hebishy, Essam</searchLink> (AUTHOR)<i> ehebishy+eic@wiley.com</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Food+Processing+%26+Preservation%22">Journal of Food Processing & Preservation</searchLink>. 6/28/2025, Vol. 2025, p1-9. 9p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Differential+scanning+calorimetry%22">Differential scanning calorimetry</searchLink><br /><searchLink fieldCode="DE" term="%22Amino+group%22">Amino group</searchLink><br /><searchLink fieldCode="DE" term="%22Viscosity+solutions%22">Viscosity solutions</searchLink><br /><searchLink fieldCode="DE" term="%22Scanning+electron+microscopy%22">Scanning electron microscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Collagen%22">Collagen</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Collagen from eggshell membrane (EM) was stabilized via a cross‐linking procedure using microbial transglutaminase as an alternative, nontoxic cross‐linking reagent for its low stability and low mechanical strength. The physicochemical features of collagen solutions (5 mg/mL), which were cross‐linked by different concentrations of MTG (30, 40, 50, 60, and 70 U/g collagen), were examined. The SDS‐PAGE, differential scanning calorimetry (DSC), residual amino group content, scanning electron microscopy (SEM), and viscosity of solutions were evaluated. The results revealed that applying higher concentrations of MTG in cross‐linked collagen solutions leads to an increase of about 32°C–39°C in denaturation temperatures (Td) and a 75.76% decrease in residual amino group content. The simultaneous effect of different temperatures and concentrations of MTG on viscosity illustrated an improvement of approximately 30 Pa·s in the viscosity of cross‐linked collagen at 50°C. The enzymatically cross‐linked porous structures displayed finer microstructure with interlinked micron‐sized pores, exhibiting a 74% reduction in size compared to the uncross‐linked collagen. These results suggest that combining MTG and EM as sources of collagen represents an innovative potential route for the safe cross‐linking of collagen‐based matrices. This innovation could have practical applications in reducing waste EM, which is a by‐product of egg breaking in industrial and domestic settings, and utilize them to produce firmness and stabilize collagen. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Food Processing & Preservation is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1155/jfpp/1786447 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 9 StartPage: 1 Subjects: – SubjectFull: Differential scanning calorimetry Type: general – SubjectFull: Amino group Type: general – SubjectFull: Viscosity solutions Type: general – SubjectFull: Scanning electron microscopy Type: general – SubjectFull: Collagen Type: general Titles: – TitleFull: Influence of Cross‐Linking by Microbial Transglutaminase on Physicochemical Properties of Eggshell Membrane Collagen. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Kazemi Kheirabadi, Elahe – PersonEntity: Name: NameFull: Kheirandish, Poorandokht – PersonEntity: Name: NameFull: Razavi, Seyed Hadi – PersonEntity: Name: NameFull: Golmakani, Mohammad-Taghi – PersonEntity: Name: NameFull: Hebishy, Essam IsPartOfRelationships: – BibEntity: Dates: – D: 28 M: 06 Text: 6/28/2025 Type: published Y: 2025 Identifiers: – Type: issn-print Value: 01458892 Numbering: – Type: volume Value: 2025 Titles: – TitleFull: Journal of Food Processing & Preservation Type: main |
| ResultId | 1 |
