Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles
(2022) In Food Chemistry: Molecular Sciences 5.- Abstract
There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO3, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t1/2 = 3 h, while the polymerization occurred with t1/2 = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed... (More)
There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO3, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t1/2 = 3 h, while the polymerization occurred with t1/2 = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate.
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- author
- Madsen, Mikkel ; Khan, Sanaullah ; Kunstmann, Sonja ; Aachmann, Finn L. ; Ipsen, Richard ; Westh, Peter ; Emanuelsson, Cecilia LU and Svensson, Birte
- organization
- publishing date
- 2022-12-30
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Dynamic light scattering, Far- and near-UV CD, Intrinsic and ANS fluorescence spectra, LC-MS/MS cross-link identification, Molecular dynamics inter-residue distance analysis, Size exclusion chromatography
- in
- Food Chemistry: Molecular Sciences
- volume
- 5
- article number
- 100137
- publisher
- Elsevier
- external identifiers
-
- scopus:85138554980
- pmid:36164490
- ISSN
- 2666-5662
- DOI
- 10.1016/j.fochms.2022.100137
- language
- English
- LU publication?
- yes
- id
- 74b1b88a-792a-4746-9a88-d9df11dce449
- date added to LUP
- 2022-12-05 16:29:03
- date last changed
- 2024-09-21 05:36:58
@article{74b1b88a-792a-4746-9a88-d9df11dce449, abstract = {{<p>There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO<sub>3</sub>, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t<sub>1/2</sub> = 3 h, while the polymerization occurred with t<sub>1/2</sub> = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate.</p>}}, author = {{Madsen, Mikkel and Khan, Sanaullah and Kunstmann, Sonja and Aachmann, Finn L. and Ipsen, Richard and Westh, Peter and Emanuelsson, Cecilia and Svensson, Birte}}, issn = {{2666-5662}}, keywords = {{Dynamic light scattering; Far- and near-UV CD; Intrinsic and ANS fluorescence spectra; LC-MS/MS cross-link identification; Molecular dynamics inter-residue distance analysis; Size exclusion chromatography}}, language = {{eng}}, month = {{12}}, publisher = {{Elsevier}}, series = {{Food Chemistry: Molecular Sciences}}, title = {{Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles}}, url = {{http://dx.doi.org/10.1016/j.fochms.2022.100137}}, doi = {{10.1016/j.fochms.2022.100137}}, volume = {{5}}, year = {{2022}}, }