Subscribe Now Subscribe Today
Research Article
 

A Microstructure of the Modeling Systems on the Basis of the Fermented Raw Material



Zinina Oksana Vladimirovna, Rebezov Maksim Borisovich and Vaiscrobova Evgeniya Sergeevna
 
Facebook Twitter Digg Reddit Linkedin StumbleUpon E-mail
ABSTRACT

A theoretical and practical interest to the expansion of the use of collagen containing raw material field in the meat foods production has been existing for many decades. But this raw material is notable in a technological respect for the unacceptable qualities that it is possible to improve by means of the biotechnological processing of the raw material. In recent years the propionic and bifidus bacteria have been drawing many scientists’ attention for the ferment processing conducting of the meat raw material. The propionic and bifidus bacteria have a high proteolytic activity and protective qualities in respect of the pathogenic and opportunistic pathogenic microflora. In this field scientists’ efforts are concentrated on the use of the mentioned bacteria in the production of fermented sausages or for the low-grade raw material softening. An aspect of using of the propionic and bifidus bacteria is studied not enough for the collagen containing raw material processing. Thereby the aim of the work is the study of the influence of the ferment processing of the collagen containing by-products of the 2nd category of bovine animals on the model systems micro structure, including protein compositions on the basis of the biomodificated by-products. In the study a detailed description of the change of the particular structural components of a model system is given when including to the model system the biomodificated raw material. It is established that under the influence of the ferment processing the decondensation of collagen fascicles occurs to particular fibrils and their fragmentation takes place. As a result when making protein compositions the homogeneous in structure emulsion comes out. Later on it is recommended to use the emulsion in boiled sausages and minced half-finished goods receipts.

Services
Related Articles in ASCI
Similar Articles in this Journal
Search in Google Scholar
View Citation
Report Citation

 
  How to cite this article:

Zinina Oksana Vladimirovna, Rebezov Maksim Borisovich and Vaiscrobova Evgeniya Sergeevna, 2016. A Microstructure of the Modeling Systems on the Basis of the Fermented Raw Material. Pakistan Journal of Nutrition, 15: 249-254.

DOI: 10.3923/pjn.2016.249.254

URL: https://scialert.net/abstract/?doi=pjn.2016.249.254

REFERENCES
1:  Adams, M.R. and L. Nicolaides, 1997. Review of the sensitivity of different foodborne pathogens to fermentation. Food Control, 8: 227-239.
CrossRef  |  Direct Link  |  

2:  Aktas, N. and M. Kaya, 2001. The influence of marinating with weak organic acids and salts on the intramuscular connective tissue and sensory properties of beef. Eur. Food Res. Technol., 213: 88-94.
CrossRef  |  Direct Link  |  

3:  Antila, M., 1954. Uber die propionsauretacterien in Emmentaler kase. Meijerit. Aikakausk, 16: 124-130.

4:  Asghar, A. and R.L. Henrickson, 1982. Chemical, biochemical, functional and nutritional characteristics of collagen in food systems. Adv. Food Res., 28: 231-272.
PubMed  |  Direct Link  |  

5:  Biavati, B., M. Vescovo, S. Torriani and V. Bottazzi, 2000. Bifidobacteria: History, ecology, physiology and applications. Ann. Microbiol., 50: 117-131.
Direct Link  |  

6:  Van Boekel, M., V. Fogliano, N. Pellegrini, C. Stanton and G. Scholz et al., 2010. A review on the beneficial aspects of food processing. Mol. Nutr. Food Res., 54: 1215-1247.
CrossRef  |  Direct Link  |  

7:  Boot-Handford, R.P. and D.S. Tuckwell, 2003. Fibrillar collagen: The key to vertebrate evolution? A tale of molecular incest. BioEssays, 25: 142-151.
CrossRef  |  Direct Link  |  

8:  Caplice, E. and G.F. Fitzgerald, 1999. Food fermentations: Role of microorganisms in food production and preservation. Int. J. Food Microbiol., 50: 131-149.
CrossRef  |  PubMed  |  Direct Link  |  

9:  Coussement, P. and A. Franck, 2001. Inulin and Oligofructose. In: Handbook of Dietary Fiber, Cho, S.S. and M.L. Dreher (Eds.). CRC Press, Boca Raton, ISBN-13: 9780203904220, pp: 721-735.

10:  Cruz, A.G., R.S. Cadena, E.H.M. Walter, A.M. Mortazavian, D. Granato, J.A.F. Faria and H.M.A. Bolini, 2010. Sensory analysis: Relevance for prebiotic, probiotic and synbiotic product development. Compr. Rev. Food Sci. Food Saf., 9: 358-373.
CrossRef  |  Direct Link  |  

11:  Djabourov, M., N. Bonnet, H. Kaplan, N. Favard, P. Favard, J.P. Lechaire and M. Maillard, 1993. 3D analysis of gelatin gel networks from transmission electron microscopy imaging. Journal de Physique Archives, 3: 611-624.
CrossRef  |  Direct Link  |  

12:  Djabourov, M., J.P. Lechaire and F. Gaill, 1993. Structure and rheology of gelatin and collagen gels. Biorheology, 30: 191-205.
PubMed  |  Direct Link  |  

13:  Veis, A., 1964. The Macromolecular Chemistry of Gelatin. Academic Press, New York.

14:  Foschino, R., A. Galli, G. Ponticelli and G. Volonterio, 1988. Propionic bacteria activity in different culture conditions. Annali Microbiologia Enzimologia, 38: 207-222.
Direct Link  |  

15:  Fujiwara, S., H. Hashiba, T. Hirota and J.F. Forstner, 1997. Proteinaceous factor(s) in culture supernatant fluids of bifidobacteria which prevents the binding of enterotoxigenic Escherichia coli to gangliotetraosylceramide. Applied Environ. Microbiol., 63: 506-512.
Direct Link  |  

16:  Geisen, R. and W.H. Holzapfel, 1996. Genetically modified starter and protective cultures. Food Microbiol., 30: 315-324.
CrossRef  |  Direct Link  |  

17:  Gomez-Gullen, M.C., B. Gimenez, M.E. Lopez-Caballero and M.P. Montero, 2011. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids, 25: 1813-1827.
CrossRef  |  Direct Link  |  

18:  Hao, M.H. and H.A. Scheraga, 1994. Statistical thermodynamics of protein folding: Sequence dependence. J. Phys. Chem., 98: 9882-9893.
CrossRef  |  Direct Link  |  

19:  Jones, E.Y. and A. Miller, 1991. Analysis of structural design features in collagen. J. Mol. Biol., 218: 209-219.
CrossRef  |  Direct Link  |  

20:  Kujawski, M., L. Lemke, Z. Bator, J. Rymaszewski and G.M. Ciehosz, 1996. Mozliwosci wynorzystania productow frmentacii propionowoej do utrwalania wendlir. Acta Acad. Agric. Ac. Technol. Dsten. Technol. Aliment., 29: 115-129.

21:  Misra, A.K. and R.K. Kuila, 1995. Antimicrobial substances from Bifidobacterium bifidum. Indian J. Dairy Sci., 48: 612-614.

22:  Rawdkuen, S. and S. Benjakul, 2012. Biochemical and microstructural characteristics of meat samples treated with different plant proteases. Afr. J. Biotechnol., 11: 14088-14095.
Direct Link  |  

23:  Rivier, N. and J.F. Sadoc, 2007. Topology in Molecular Biology. Springer, New York, USA., pp: 147-162.

24:  Steinkraus, K.H., 2004. Origin and History of Food Fermentations. In: Handbook of Food and Beverage Fermentation Technology, Hui, Y.H., L. Meunier-Goddik, A.S. Hansen, J. Josephsen, W.K. Nip, P.S. Stanfeld and F. Toldra (Eds.). Marcel Dekker, Inc., New York, USA., pp: 1-9.

25:  Wess, T.J., 2008. Collagen Fibrillar Structure and Hierarchies. In: Collagen: Structure and Mechanics, Fratzl, P. (Ed.). Chapter 3, Springer, USA., ISBN: 978-0-387-73905-2, pp: 49-80.

26:  Yuksekdag, Z.N., D.O. Darilmaz and Y. Beyatli, 2014. Dairy propionibacterium strains with potential as biopreservatives against foodborne pathogens and their tolerance-resistance properties. Eur. Food Res. Technol., 238: 17-26.
CrossRef  |  Direct Link  |  

©  2020 Science Alert. All Rights Reserved