Enzymatic cross-linking of β-lactoglobulin in solution and at air–water interface: Structural constraints

Dilek Ercili-Cura; Riitta Partanen; Fiona Husband; Mike Ridout; Adam Macierzanka; Martina Lille; Harry Boer; Raija Lantto; Johanna Buchert; Alan Mackie

doi:10.1016/j.foodhyd.2011.11.010

Enzymatic cross-linking of β-lactoglobulin in solution and at air–water interface: Structural constraints

Abstract

Effective and controlled use of cross-linking enzymes in structure engineering of food systems depends on characterization of the favorable conditions for enzyme-substrate complex and the limiting factors for the desired modification. In this respect, we analyzed the susceptibility of bovine β-lactoglobulin (BLG) to enzymatic cross-linking by Trichoderma reesei tyrosinase (TrTyr) and transglutaminase (TG). Changes in BLG molecular structure were determined at pH 6.8, 7.5 and 9.0 before and after high-temperature heat treatment. The conformational change was linked to efficiency of protein cross-linking. BLG was not susceptible to TrTyr without heat treatment. TG, however, induced inter-molecular cross-links at pH 7.5 and 9.0. After the heat treatments, BLG molecules adopted a molten-globule-like conformation. Both of the enzymes were able to form inter-molecular cross-links between heat-denatured BLG molecules. Electrophoretic mobility and broadness of the oligomer bands created by both enzymes on SDS-PAGE gels showed differences which were linked to the availability and number of target amino acid residues. Evidence for intra-molecular cross-linking was obtained. Once adsorbed to air/water interface, BLG formed a viscoelastic surface film which was characterized by surface shear rheology. Application of cross-linking enzymes under a dense layer of BLG molecules at the interface led to decreasing G′ with time. Intra-molecular links were most probably favored against inter-molecular on packed BLG layer leading to constrained molecules. Results in general emphasize the importance of structural and colloidal aspects of protein molecules in controlling inter/intra-molecular bond formation by cross-linking enzymes.

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Authors (10)

Dilek Ercili-Cura
Riitta Partanen
Fiona Husband
Mike Ridout
Adam Macierzanka dr hab. inż.
- Norwich Research Park
Martina Lille
Harry Boer
Raija Lantto
Johanna Buchert
Alan Mackie

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Details

Category:: Articles
Type:: artykuł w czasopiśmie wyróżnionym w JCR
Published in:: FOOD HYDROCOLLOIDS no. 28, edition 1, pages 1 - 9,
ISSN: 0268-005X
Language:: English
Publication year:: 2012
Bibliographic description:: Ercili-Cura D., Partanen R., Husband F., Ridout M., Macierzanka A., Lille M., Boer H., Lantto R., Buchert J., Mackie A.: Enzymatic cross-linking of β-lactoglobulin in solution and at air–water interface: Structural constraints// FOOD HYDROCOLLOIDS. -Vol. 28, iss. 1 (2012), s.1-9
DOI:: Digital Object Identifier (open in new tab) 10.1016/j.foodhyd.2011.11.010
Verified by:: Gdańsk University of Technology