Emulsifying Properties of Milk Proteins Cross-linked with Microbial Transglutaminase

Færgemand, M.; Otte, Jeanette; Qvist, K.B.

doi:10.1016/s0958-6946(98)00111-3

Cited by 87 publications

(71 citation statements)

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“…As expected, these cross-linking reactions led to modifications of functional properties of caseins such as solubility, emulsifying capacity, foaming, and gelation properties (Motoki et al 1984;Nio et al 1986;Faergemand and Qvist 1997;Nonaka et al 1997;Faergemand et al 1998;Ozer et al 2007). Cross-linking of casein micelles improved their intra-micellar stability.…”

Section: Reticulationsupporting

confidence: 63%

Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

264

133

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Casein molecules are used in food industry as ingredients. They can be used as isolated forms and under micellar form consisting in an association of different casein molecules and calcium phosphate. In this review, after a brief reminder of the main characteristics of casein molecules and casein micelles, the modifications of caseins induced by physical, chemical, and enzymatic actions are reported. The resulting new physicochemical properties (mineral and casein compositions, charge, hydrophobicity, aggregation state, and morphology) and techno-functionalities (heat stability, viscosity, gelation, emulsifying, and foaming properties) are described and discussed with a special attention paid to the results obtained in our laboratory since several decades.

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Section: Reticulationsupporting

confidence: 63%

Modifications of structures and functions of caseins: a scientific and technological challenge

Broyard

Gaucheron

2015

Dairy Sci. & Technol.

264

133

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“…The creaming stability of milk protein stabilized emulsions was improved even with relatively extensive cross-linking. This was ascribed to changes in the adsorbed layer or increased viscosity of the continuous phase (Faergemand, Otte, & Qvist, 1998). A reduced creaming of sodium caseinate stabilized oil/water emulsions was also detected by Lorenzen (2000).…”

Section: Introductionmentioning

confidence: 70%

Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients

Lorenzen¹

2007

Food Research International

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“…Improved crosslinking without a mediator may be more likely obtained after homogenization of the protein. During homogenization, the protein adsorbs to the oil droplet surface and tyrosine residues can become more exposed and available to the enzyme's active site, leading to a higher crosslinking rate (Faergemand, Otte, & Qvist, 1998). Therefore, homogenization was performed prior to crosslinking in the absence of caffeic acid.…”

Section: Crosslinking After Homogenization In the Absence Of Caffeicmentioning

confidence: 99%

Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin

et al. 2015

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a b s t r a c tThe effect of crosslinked soy glycinin with tyrosinase from Bacillus megaterium (TyrBm) on o/w emulsion properties was studied. The ability of TyrBm to crosslink soy glycinin was evaluated in the presence or absence of three phenolic mediators. It was observed that crosslinking of glycinin is facilitated by a phenolic mediator and is negligible in its absence. Subsequently, the glycinin-stabilized emulsions were evaluated in two systems: (i) homogenization after crosslinking in the presence of a mediator, caffeic acid, and (ii) homogenization prior to crosslinking in the absence of caffeic acid. Emulsions were prepared using a high-pressure homogenizer and their particle size, creaming resistance, viscosity and microstructure were measured. Results indicate that the method of emulsion preparation affected the emulsion physical stability, thus, the first system led to a decrease in emulsion stability against creaming while the second system resulted with improved properties after the enzymatic treatment; Crosslinking after homogenization eliminated the need for a phenolic mediator and led to a lower creaming velocity and higher viscosity. In addition, fluorescence microscopy observations demonstrated that the crosslinking reaction of TyrBm after homogenization led to the formation of cold-set gel-like structures of small droplets linked by covalent bonds.

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Emulsifying Properties of Milk Proteins Cross-linked with Microbial Transglutaminase

Cited by 87 publications

References 0 publications

Modifications of structures and functions of caseins: a scientific and technological challenge

Modifications of structures and functions of caseins: a scientific and technological challenge

Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients

Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin

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