Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation

Schorsch, Catherine; Carrié, Hélène; Norton, Ian T.

doi:10.1016/s0958-6946(00)00069-8

Cited by 116 publications

(77 citation statements)

References 17 publications

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“…It can be seen in Figure 1 that κ-casein in the milk micelle system is a good substrate for Tgase. Schorsch et al [37] suggested that Tgase prevented disaggregation of casein micelles on acidification. Tgase-induced cross-linking between casein molecules at the surface of the micelle probably impaired the mobility and flexibility of the κ-casein ''hairs'', reducing the volume spanned by the κ-casein and lessening its effects of steric stabilisation.…”

Section: Effect Of Tgase On the Properties Of Micellar Casein On Acidmentioning

confidence: 99%

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 Properties Of Micellar Casein On Acidmentioning

confidence: 99%

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

Mounsey

O’Kennedy

Kelly

2005

Lait

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Milk gels have both traditional and high commercial value within the dairy industry (Schorsch et al 2000;Siamand et al 2014). Besides renneting, acidification of milk is the most routine way to form milk protein gels.

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confidence: 99%

“…TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al 2013), and thus improve water retention (Schorsch et al 2000;Ercili-Cura et al 2013) and texture (Ercili-Cura et al 2010) of protein gels.…”

mentioning

confidence: 99%

“…Moreover, it was also observed that the GC-caseinate gels had the higher final tan δ value (0.30) than caseinate and cross-linked caseinate gels (0.15 or 0.10) ( Figure 3B). Hydrogen bonds, belonging to the most important forces involved in the interaction of protein molecules, can take part in protein gelation (Schorsch et al 2000). GC-caseinate contained saccharide groups in its molecules whilst neither caseinate nor cross-linked caseinate had any saccharide groups.…”

mentioning

confidence: 99%

“…These results support that the gels from GC-caseinate and crosslinked caseinate should have the highest and lowest WHC, respectively. It has been proved that caseinate cross-linking results in a homogeneous gel network (Faergemand & Qvist 1997;Schorsch et al 2000).…”

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confidence: 99%

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Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

Song¹,

Zhao²

2016

Czech J. Food Sci.

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Milk gels have both traditional and high commercial value within the dairy industry (Schorsch et al. 2000;Siamand et al. 2014). Besides renneting, acidification of milk is the most routine way to form milk protein gels. Acidifying milk using glucono-δ-lactone (GDL) can slowly form structured gel products (Lucey 2004). Two major steps are involved in the formation of the acidified milk gels. In the first step, a collapse of the hairy brush of the casein micelles occurs, and the colloidal calcium and phosphate are then dissolved out of the casein micelle as a result of the protonation of ionised phosphate groups (Gaygadzhiev et al. 2009). Micellar structure is thus profoundly altered but without dissociation. In the second step, at a pH value about 5.0, casein precipitates isoelectrically, or under quiescent conditions it forms rather fragile gels (Lucey 2004). The balance between attractive and repulsive forces within protein molecules results in gel formation (Havea 2006;Rocha et al. 2009). Both intrinsic (e.g. amino acid compositions, molecular weights, hydrophobicity, etc.) and extrinsic (protein concentrations, pH value, temperature, metal ions, and ionic strengths) factors all show impacts on gelation and physiochemical properties of protein gels.During the last years, transglutaminase (TGase, EC 2.3.2.13) has been used to modify proteins via inducing protein cross-linking (between glutamine and lysine residues of the proteins) (Anema & Kruif 2012;Domagała et al. 2015). TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al. 2013), and thus improve water retention (Schorsch et al. 2000;Ercili-Cura et al. 2013) and texture (Ercili-Cura et al. 2010) of protein gels. 564Food Technology and Economy, Engineering and Physical Properties Czech J. Food Sci., 34, 2016 (6) Caseinate, transglutaminase (TGase), and an oligochitosan of 1 kDa were used to prepare a glycated and cross-linked caseinate (GC-caseinate), aiming to assess potential changes in both the structure and gelling properties of such caseinate. The results of Fourier transform infrared analysis revealed that only GC-caseinate contained saccharide portions in its molecules, evidencing TGase-induced caseinate glycation. Circular dichroism results showed that GC-caseinate possessed a more ordered secondary structure than caseinate. Other results also demonstrated that TGase-induced modification resulted in a lower gelation temperature of GC-caseinate (59°C vs. 68°C) and increased the final tan δ value (0.30 vs. 0.15) compared to caseinate during the development of acidified gels. In addition, the acidified gels from GC-caseinate were detected to have lower water holding capacity (0.720 vs. 0.781 g/g gels), expanded gel network, and larger pore sizes than those from caseinate. It is thus evidenced that the used TGase-induced modification could confer caseinate with ordered secondary structure, expanded gel network but lower water holding capacity.

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Crosslinking of casein by microbial transglutaminase and its resulting influence on the stability of micelle structure

Partschefeld

Schwarzenbolz

Richter

et al. 2007

Biotechnology Journal

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The influence of enzymatic crosslinking by microbial transglutaminase (mTG) on the stability of casein micelles of ultrahigh temperature (UHT)-treated milk in the presence of EDTA (0-0.45 mM) or ethanol (0-74 vol%) as well as under high hydrostatic pressures up to 400 MPa was investigated. Disintegration of micelles and changes in micelle size were monitored by the measurement of turbidity as well as by dynamic light scattering. The results show that the incubation of UHTtreated milk with mTG resulted in an improved micelle stability toward disintegration on addition of EDTA, ethanol, or pressure treatment. Intramicellar formed isopetides significantly enhanced the stability of casein micelles. It is supposed that net-like crosslinks are formed within the external region of the micelles and they adopt the stabilizing role of colloidal calcium phosphate within the micelles, thus making the micelles less contestable for disrupting influences.

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Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation

Cited by 116 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

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

Crosslinking of casein by microbial transglutaminase and its resulting influence on the stability of micelle structure

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