Skip to main content
Log in

Physicochemical Properties of Mammalian Gelatin in Relation to Membrane Process Requirement

  • Communication
  • Published:
Food and Bioprocess Technology Aims and scope Submit manuscript

Abstract

In any of the membrane process application, understanding of the characteristics of the feed solution is essential in order to achieve desired level of separation performance. In this study, in an effort to substitute evaporation with membrane processes partially, experiments were carried out to investigate the physicochemical properties of gelatins, namely, molecular weight distribution, pH, viscosity, isoelectric point, and gel strength, which are, of foremost, important parameters in the characterization of gelatin. Two different mammalian gelatins, i.e. from bovine (type B) and porcine (type A) sources, were used in this study. The pH was significantly varied for all gelatins in the vicinity of 4.75–5.51 (±0.01). Experimental result revealed that both sources of mammalian gelatin contained components of different molecular weights with wide distribution ranging from 10 to 400 kDa. Analysis of the molecular weight distribution result also showed strong correlation between average molecular weight and gel strength of gelatin. The isoelectric points of gelatins from bovine were 4.60 ± 0.08 to 5.25 ± 0.43 and porcine gelatins were in the range of 7–9.3, which agreed well with the results obtained from other researchers. The high bloom strength mammalian gelatins were also significantly more viscous and thus, had a higher melting point.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

References

  • Agilent Technologies, Inc. (2008). Agilent High Sensitivity Protein 250 Kit Guide. Available at: www.agilent.com/chem/labonachip. Accessed 31 March 2009.

  • Arnesen, J. A., & Gildberg, A. (2002). Preparation and Characterization of Gelatin From the Skin of Harp Seal (Phoca groendlandica). Bioresource Technology, 82, 191–194.

    Article  CAS  Google Scholar 

  • Arnesen, J. A., & Gildberg, A. (2007). Extraction and characterisation of gelatin from Atlantic salmon (Salmo salar) skin. Bioresource Technology, 98, 53–57.

    Article  CAS  Google Scholar 

  • British Standards Institution. (1975). Methods for sampling and testing gelatin (physical and chemical methods). London: BSI.

    Google Scholar 

  • Chakravorty, B., & Singh, D. P. (1990). Concentration and purification of gelatin liquor by ultrafiltration. Desalination, 78, 279–286.

    Article  CAS  Google Scholar 

  • Choi, S.-S., & Regenstein, J. M. (2000). Physicochemical and sensory characteristics of fish gelatin. Journal of Food Science, 65(2), 194–199.

    Article  CAS  Google Scholar 

  • Dutré, B., & Trägårdh, G. (1995). Purification of gelatin with a forced solvent stream along the membrane permeate side: an experimental approach. Journal of Food Engineering, 25, 233–244.

    Article  Google Scholar 

  • Gómez-Guillén, M. C., Turnay, J., Fernandez-Diaz, M. D., Ulmo, N., Lizarbe, M. A., & Montero, P. (2002). Structural and physical properties of gelatin extracted from different marine species—a comparative study. Food Hydrocolloids, 16, 25–34.

    Article  Google Scholar 

  • Haug, I. J., Draget, K. I., & Smidsrød, O. (2004). Physical and rheological properties of fish gelatin compared to mamalian gelatin. Food Hydrocolloids, 18, 203–213.

    Article  CAS  Google Scholar 

  • Jamilah, B., & Harvinder, K. G. (2001). Properties of gelatins from skins of fish—black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Chemistry, 77, 81–84.

    Article  Google Scholar 

  • Johnston-Banks, F. A. (1990). Gelatin. In P. Harris (Ed.), Food gels (pp. 233–289). London: Elsevier Appl Food Sci Publ.

    Google Scholar 

  • Marshall, A. D., Munro, P. A., & Trägardh, G. (1993). The effect of protein fouling in microfiltration and ultrafiltration on permeate flux, protein retention and selectivity: a literature review. Desalination, 91, 65.

    Article  CAS  Google Scholar 

  • Morrison, N. A., Clark, R. C., Chen, Y. L., Talashek, T., & Sworn, G. (1999). Gelatin alternatives for the food industry. In K. Nishinari, F. Kremer & G. Lagaly (Eds.), Physical chemistry and industrial application of gellan gum (pp. 127–131). Heidelberg: Springer-Verlag.

    Chapter  Google Scholar 

  • Norland, R. E. (1990). Fish gelatin. In M. N. Voigt & J. K. Botta (Eds.), Advances in fisheries and biotechnology for increased profitability (pp. 325–333). Lancaster: Technomic.

    Google Scholar 

  • Ogawa, M., Moody, M. W., Portier, R. J., Bell, J., Schexnayder, M. A., & Losso, J. N. (2004). Biochemical properties of bone and scale collagens isolated from the subtropical fish black drum (Pogonia cromis) and sheepshead seabream (Archosargus probatocephalus). Food Chemistry, 88, 495–501.

    Article  CAS  Google Scholar 

  • Queiroz, V., & Fontes, S. (2008). Experimental analysis of structural change and rheological behavior of macromolecular solutions with guar and xanthan gums in crossflow microfiltration processing. Food and Bioprocess Technology, 1(2), 180–186.

    Article  Google Scholar 

  • Rai, C., Rai, P., Majumdar, G., De, S., DasGupta, S. (2008). Mechanism of permeate flux decline during microfiltration of watermelon (Citrullus lanatus) juice. Food and Bioprocess Technology, DOI: 10.1007/s11947-008-0118-2

  • Schrieber, R., & Gareis, H. (2007). Gelatine handbook—theory and industrial practice. Germany: Wiley.

    Google Scholar 

  • Simon, A., Vandanjon, L., Levesque, G., & Bourseau, P. (2002). Concentration and desalination of fish gelatin by ultrafiltration and continuous diafiltration process. Desalination, 144, 313–318.

    Article  CAS  Google Scholar 

  • Skelton, R. (1986). Membrane technology: technical and applications brief. London: Paper presented at a meeting of the Society of Chemical Industry.

    Google Scholar 

  • US, F. D. A. (1997). FDA Center of Biologics Evaluation and Research. Transcript of Meeting April: Transmissible Spongiform Encephalopathies Advisory Committees. 23.

    Google Scholar 

  • Veis, A. (1964). The macromolecular chemistry of gelatin. New York: Academic.

    Google Scholar 

  • Ward, A. G., & Courts, A. (1977). The science and technology of gelatin. London: Academic.

    Google Scholar 

  • Yoshimura, K., Terashima, M., Hozan, D., Ebato, T., Nomura, Y., Ishii, Y., et al. (2000). Physical properties of shark fin gelatin compared with pig gelatin. Journal of Agricultural Food Chemistry, 48, 2023–2027.

    Article  CAS  Google Scholar 

  • Zhang, Z. K., Li, G. Y., & Shi, B. (2005). Physicochemical properties of collagen, gelatin and collagen hydrolysate derived from bovine limed split wastes. Journal of the Society of Leather Technologists and Chemists, 90, 23–28.

    Google Scholar 

Download references

Acknowledgment

The authors would like to acknowledge the financial grant funded by Universiti Kebangsaan Malaysia via grant UKM-GUP-KPB-08-32-129 and TF0206A084. The authors would also like to acknowledge Halagel (M) Sdn Bhd for their donation of the gelatin.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Abdul Wahab Mohammad.

Additional information

Ying Pei Lim was on study leave from Faculty of Chemical Engineering, Universiti Teknologi MARA, 40450 Shah Alam, Selangor, Malaysia.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lim, Y.P., Mohammad, A.W. Physicochemical Properties of Mammalian Gelatin in Relation to Membrane Process Requirement. Food Bioprocess Technol 4, 304–311 (2011). https://doi.org/10.1007/s11947-009-0285-9

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11947-009-0285-9

Keywords

Navigation