Wyszukiwarka
Enzymatic cross-linking of β-lactoglobulin in solution and at air–water interface: Structural constraints
Abstrakt
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.
Cytowania
-
3 5
CrossRef
-
0
Web of Science
-
3 6
Scopus
Autorzy (10)
-
Dilek Ercili-Cura
-
Riitta Partanen
-
Fiona Husband
-
Mike Ridout
-
-
Martina Lille
-
Harry Boer
-
Raija Lantto
-
Johanna Buchert
-
Alan Mackie
Cytuj jako
Pełna treść
pełna treść publikacji nie jest dostępna w portalu
Słowa kluczowe
Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuł w czasopiśmie wyróżnionym w JCR
- Opublikowano w:
-
FOOD HYDROCOLLOIDS
nr 28,
wydanie 1,
strony 1 - 9,
ISSN: 0268-005X - Język:
- angielski
- Rok wydania:
- 2012
- Opis bibliograficzny:
- 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:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1016/j.foodhyd.2011.11.010
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 111 razy
Publikacje, które mogą cię zainteresować
Which casein in sodium caseinate is most resistant to in vitro digestion? Effect of emulsification and enzymatic structuring
- B. Franziska,
- D. Didier,
- D. Dulko
- + 3 autorów
Emulsification alters simulated gastrointestinal proteolysis of β-casein and β-lactoglobulin
- A. Macierzanka,
- A. Sancho,
- E. Mills
- + 2 autorów