Skip to main content Accessibility help
×
Home
Hostname: page-component-768ffcd9cc-jpcp9 Total loading time: 0.194 Render date: 2022-12-06T01:42:55.502Z Has data issue: true Feature Flags: { "useRatesEcommerce": false } hasContentIssue true

Porcine β-lactoglobulin does not undergo thermally induced gelation

Published online by Cambridge University Press:  01 June 2009

Daniel P. Gallagher
Affiliation:
Department of Food Chemistry, National Food Biotechnology Centre, University College, Cork, Irish Republic
M. Gerard Lynch
Affiliation:
Department of Food Chemistry, National Food Biotechnology Centre, University College, Cork, Irish Republic
Daniel M. Mulvihill
Affiliation:
Department of Food Chemistry, National Food Biotechnology Centre, University College, Cork, Irish Republic

Abstract

Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
Short Communications
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Alexander, L. J. & Beattie, C. W. 1992 Sequence of porcine β-lactoglobulin cDNA. Animal Genetics 23 263265CrossRefGoogle ScholarPubMed
AOAC 1970 Official Methods of Analysis of the Association of Official Analytical Chemists, 11th edn, p. 248. Washington, DC: AOACGoogle Scholar
Bevekidge, T., Toma, S. J. & Nakai, S. 1974 Determination of SH– and SS– groups in some food proteins using Ellman's reagent. Journal of Food Science 39 4951CrossRefGoogle Scholar
Dalgalarrondo, M., Dufour, E., Bertrand-Harb, C., Chobert, J. M. & Haertlé, T. 1992 Purification and characterization of two porcine β-lactoglobulin variants by NaCl salting-out and reversed phase HPLC. Lait 72 3542CrossRefGoogle Scholar
Greaser, M. L., Yates, L. D., Krzywicki, K. & Roelke, D. L. 1983 Electrophoretic methods for the separation and identification of muscle proteins. Proceedings, 36th Reciprocal Meat Conference 38 8791Google Scholar
Kessler, E. & Brew, K. 1970 The whey proteins of pig's milk: isolation and characterization of a β-lactoglobulin. Biochimica et Biophysica Ada 200 449458CrossRefGoogle ScholarPubMed
Kuwajima, K. 1989 The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Structure, Function and Genetics 6 87103CrossRefGoogle ScholarPubMed
Lee, S. P., Cho, Y. J. & Batt, C. A. 1993 Enhancing the gelation of β-lactoglobulin. Journal of Agricultural and Food Chemistry 41 13431348CrossRefGoogle Scholar
McSwiney, M., Singh, H., Campanella, O. & Creamer, L. K. 1994 Thermal gelation and denaturation of bovine β-lactoglobulins A and B. Journal of Dairy Research 61 221232CrossRefGoogle Scholar
Matsudomi, N., Rector, D. & Kinsella, J. E. 1991 Gelation of bovine serum albumin and β-lactoglobulin; effects of pH, salts and thiol reagents. Food Chemistry 40 5569CrossRefGoogle Scholar
Morris, E. R. & Ross-Murphy, S. B. 1981 Chain flexibility of polysaccharides and glycoproteins from viscosity measurements. Techniques in the Life Sciences B308310146Google Scholar
Mulvihill, D. M. & Kinsella, J. E. 1987 Gelation characteristics of whey proteins and β-lactoglobulin. Foal Technology 41 (9) 102, 104, 100, 108, 110111Google Scholar
Mulvihill, D. M., Rector, D. & Kinsella, J. E. 1991 Mercaptoethanol, N-ethylmalcimide, propylene glycol and urea effects on rheological properties of thermally induced β-lactoglobulin gels at alkaline pH. Journal of Food Science 56 13381341CrossRefGoogle Scholar
Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. T., Findlay, J. B. C., Sivaprasadarao, R., Jones, T. A., Newcomer, M. E. & Kraulis, P. J. 1986 The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324 383385CrossRefGoogle ScholarPubMed
Shimada, K. & Matsushita, S. 1980 Relationship between thermocoagulation of proteins and amino acid compositions. Journal of Agricultural and Food Chemistry 28 413417CrossRefGoogle Scholar
Stading, M. & Hermansson, A. M. 1990 Viscoelastic behaviour of β-lactoglobulin gel structures. Food Hydrocolloids 4 121135CrossRefGoogle Scholar
9
Cited by

Save article to Kindle

To save this article to your Kindle, first ensure coreplatform@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Porcine β-lactoglobulin does not undergo thermally induced gelation
Available formats
×

Save article to Dropbox

To save this article to your Dropbox account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you used this feature, you will be asked to authorise Cambridge Core to connect with your Dropbox account. Find out more about saving content to Dropbox.

Porcine β-lactoglobulin does not undergo thermally induced gelation
Available formats
×

Save article to Google Drive

To save this article to your Google Drive account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you used this feature, you will be asked to authorise Cambridge Core to connect with your Google Drive account. Find out more about saving content to Google Drive.

Porcine β-lactoglobulin does not undergo thermally induced gelation
Available formats
×
×

Reply to: Submit a response

Please enter your response.

Your details

Please enter a valid email address.

Conflicting interests

Do you have any conflicting interests? *