Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels

Schorsch, Catherine; Carrié, Hélène; Clark, Allan H.; Norton, Ian T.

doi:10.1016/s0958-6946(00)00052-2

Cited by 69 publications

(67 citation statements)

References 17 publications

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“…In agreement with these particle size results and the findings of Schorsch et al [36], dynamic rheological evaluation of Tgase-incubated micellar casein (results not shown) showed the absence of gelation at neutral pH.…”

Section: Effect Of Tgase On the Propertiessupporting

confidence: 92%

“…Heated samples were immediately placed in a water bath at 78°C for 30 min to inactivate the enzyme and subsequently cooled to 22°C. This heat treatment is the same as used by Murphy et al [26] on β-lactoglobulin solutions to provide maximal exposure of reactive thiol (-SH) groups and should have been sufficient to inactivate the Tgase, which inactivates in less than 1 min at 80°C [36]. Control samples had no enzyme addition and/or heat treatment.…”

Section: Preparation Of Protein Dispersionsmentioning

confidence: 99%

“…In addition, the degree of aggregation of the protein substrate prior to incubation with the enzyme may have significant effects on any eventual functionality. Schorsch et al [36] showed that when transglutaminase was added to skimmed milk at pH 6.7, no gel formation was observed. This inability to gel was attributed to electrostatic and/ or steric repulsion between the protein particles, caused by a layer of κ-casein on the surface.…”

Section: Introductionmentioning

confidence: 99%

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Influence of transglutaminase treatment on properties of micellar casein and products made therefrom

Mounsey

O’Kennedy

Kelly

2005

Lait

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-This work investigated the effect of transglutaminase on (1) micellar casein (phosphocasein) suspensions at pH 6.7; (2) gel formation at pH 4.6; and (3) viscosity of the subsequently produced sodium caseinates. Micellar casein (25 g protein·kg -1 in simulated milk ultrafiltrate, pH 6.7) was incubated with and without 1% microbial transglutaminase (Tgase) at 40°C for 5-60 min, prior to thermal inactivation (78°C × 30 min). The particle size of micellar casein incubated with Tgase (mean between treatments of 213 nm) was not markedly different from the control micellar casein (195 nm), indicating very little inter-micellar cross-linking. Heat stability was markedly improved at pH > 6.8 following incubation with Tgase. When Tgase was not inactivated prior to acidification gels were markedly stronger. The maximum in casein hydration (pH 5.2-5.5) and tan δ (pH 5.0) were eliminated by the action of Tgase indicating a loss of casein mobility. In the absence of Tgase, a sodium caseinate suspension had a low apparent viscosity of 7.6 mPa·s (100 s -1 ) with Newtonian behaviour, low turbidity (A 600nm = 0.28 and an ethanol stability of 530 mL·L -1 ). Sodium caseinate could not be produced where the Tgase was active during the acidification step. Sodium caseinate made from micellar casein treated with Tgase (5 min) showed increased viscosity (64.6 mPa·s at 100 s -1 ), turbidity (A 600nm = 1.37) and ethanol stability (621 mL·L -1 ). With the exertion of proper control, Tgase can improve some of the functional properties of micellar casein or its sodium caseinate derivative.high viscosity / sodium caseinate / transglutaminase / milk protein Résumé -Influence de la transglutaminase sur les propriétés de la caséine micellaire et de ses produits dérivés. L'effet de la transglutaminase sur (1) des suspensions de caséine micellaire (phosphocaséine) à pH 6,7; (2) la formation de gel à pH 4,6; et (3) la viscosité du caséinate de sodium obtenu par la suite, était étudié. La caséine micellaire (25 g protéine·kg -1 dans un ultrafiltrat de lait simulé, pH 6,7) était incubée en présence ou non de 1 % de transglutaminase (Tgase) d'origine microbienne à 40 °C pendant 5-60 min, avant inactivation thermique (78 °C × 30 min). La taille des particules de caséine micellaire incubée avec la Tgase (moyenne de 213 nm entre traitements) n'était pas considérablement différente de celle du contrôle de caséine micellaire (195 nm), indiquant de très faibles liaisons inter-micellaires. La stabilité thermique était considérablement améliorée à pH > 6,8 après incubation avec la Tgase. Quand la Tgase n'était pas inactivée avant acidification, les gels étaient considérablement plus forts. Les maxima d'hydratation de la caséine (pH 5,2-5,5) et tan δ (pH 5,0) étaient éliminés par l'action de la Tgase indiquant une perte de mobilité de la caséine. En absence de Tgase, une suspension de sodium de caséinate avait une faible viscosité apparente de 7,6 mPa·s (100 s -1 ) avec un comportement Newtonien, une faible turbité (A 600nm = 0,28) et une stabilité à...

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Section: Effect Of Tgase On the Propertiessupporting

confidence: 92%

Section: Preparation Of Protein Dispersionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Influence of transglutaminase treatment on properties of micellar casein and products made therefrom

Mounsey

O’Kennedy

Kelly

2005

Lait

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“…Cross-linking causes surface changes on the casein micelles and alters the interactions between the micelles (Ercili Cura et al, 2009;Schorsch, Carrie, Clark, & Norton, 2000). Thus, treatment of the whole milk by the ternary system in the present study would result in the treated yoghurt different microstructural characteristics than the control yoghurt.…”

Section: Microstructural Characteristics Of Yoghurt Samplesmentioning

confidence: 85%

Quality attributes of the set-style yoghurt from whole bovine milk as affected by an enzymatic oxidative cross-linking

Chang

Kong

Zhao

2014

CyTA - Journal of Food

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“…The addition of MTG causes the formation of gels with covalent bonds as additional stabilising elements, which, depending on parameters like pH and temperature [4], affect gel rheology and stabilise colloidal properties [5]. Transglutaminase induces the cross-linking of casein, leading to an increase in molecular weight [2].…”

Section: Introductionmentioning

confidence: 99%

Casein gelation under simultaneous action of transglutaminase and glucono‐δ‐lactone

Menéndez

Schwarzenbolz

Rohm

et al. 2004

Nahrung

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Casein solutions (5% w/v) were treated with microbial transglutaminase (MTG) and glucono-delta-lactone (GDL) under varying conditions in order to obtain gels. Storage modulus (G') and gelation time of the gels were measured by oscillation rheometry, while protein cross-linking was determined by gel permeation chromatography. The addition of only GDL to milk resulted in very weak gels, while MTG on its own was not able to create gel networks. Simultaneous action of both ingredients led to gels, the firmness of which was linearly related to the added amount of MTG, but passed through a maximum with rising GDL concentrations. Using chromatographical analysis, increasing G' values were interrelated with the formation of MTG-induced oligomers. The gelation time was directly proportional to the GDL concentration but not influenced by the addition of MTG within the studied range of concentration.

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Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels

Cited by 69 publications

References 17 publications

Influence of transglutaminase treatment on properties of micellar casein and products made therefrom

Influence of transglutaminase treatment on properties of micellar casein and products made therefrom

Quality attributes of the set-style yoghurt from whole bovine milk as affected by an enzymatic oxidative cross-linking

Casein gelation under simultaneous action of transglutaminase and glucono‐δ‐lactone

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