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Chicken Pepsin and Rennet Gels: Internal Bonds, Rheology and Microstructure | OMICS International | Abstract
ISSN: 2157-7579

Journal of Veterinary Science & Technology
Open Access

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Research Article

Chicken Pepsin and Rennet Gels: Internal Bonds, Rheology and Microstructure

Ferial Aziza Benyahia-Krid1*, Ouarda Aissaoui-Zitoun1, Halima Boughellout1, Faiza Adoui1, El Hocine Siar1, Abdellah Zikiou2, Attia Hamadi3 and Mohamed Nasser Eddine Zidoune1

1Laboratory of Nutrition and Food Technology, INATAA, University of Mentouri Brothers of Constantine 1, Ain El Bay Street, Constantine, 25000, Algeria

2Centre de Biotechnologie, Division Biotechnologie Alimentaire, Constantine, 25000, Algeria

3Département de biologie, Laboratoire Analyses Alimentaires, Ecole Nationale d’Ingénieurs de Sfax, Route de Soukra, ENIS, BPW, 3038 Sfax, Tunisia

*Corresponding Author:
Ferial Aziza Benyahia-Krid
Institute of the Nutrition, The Foods Technologies (INATAA)
University of Mentouri Brothers of Constantine 1
UMC, Ain El Bay Street 25000
Constantine, Algeria
Tel: +21331600242
E-mail: [email protected]

Received date: July 30, 2016; Accepted date: August 15, 2016; Published date: August 19, 2016

Citation: Benyahia-Krid FA, Aissaoui-Zitoun O, Boughellout H, Adoui F, Harkati A, et al. (2016) Chicken Pepsin and Rennet Gels: Internal Bonds, Rheology and Microstructure. J Vet Sci Technol 7: 375. doi: 10.4172/2157-7579.1000375

Copyright: © 2016 2016 Benyahia-Krid FA, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


The internal bonds created in milk gelation with chicken pepsin were approached by the use of dissociating agents-sodium dodecyl sulfate (SDS), urea, ethylenediamine tetraacetic acid (EDTA) and compared to those with rennet gel. Gels viscoelasticity aspects and microstructure were studied using rheological dynamic non-destructive measurements and Scanning Electron Microscopy (SEM) respectively. Results showed that no significant differences (p>0.05) in protein interactions between the two types of gel, with hydrophobic binding dominance in protein gelation. Viscoelasticity and microstructure also showed a similarity in the viscoelastic properties and in milk aggregation micelles mode, obtained by chicken pepsin or rennet.