Enzymatic cross-linking of whey proteins by a Ca2+-independent microbial transglutaminase from Streptomyces lydicus

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

doi:10.1016/s0268-005x(97)80006-9

Cited by 95 publications

(59 citation statements)

References 24 publications

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“…Similar particle sizes were obtained by Vasbinder et al [45] for Tgasetreated micellar casein in water. In agreement with Faergemand and Qvist [7], this would suggest that enzyme-induced intermicellar cross-linking is not a major occurrence under these conditions of pH, ionic strength, protein concentration and aggregation-state.…”

Section: Effect Of Tgase On the Propertiessupporting

confidence: 88%

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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: 88%

“…Milk proteins, especially casein, have the potential to be good substrates for crosslinking by transglutaminase [6,7,38]. Cross-linking of proteins results in the formation of dimers, trimers and larger protein polymers.…”

Section: Introductionmentioning

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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“…Similar observation had been noted by Truong et al [2004], who reported that the protein network was partially formed during the enzymatic polymerization, requiring less heat for the protein gelation with TGase treatment whereas the gel point temperature of WPI solutions treated with 0.12 unit of immobilized TGase/g was slightly decreased. Gelation was observed visually in the enzyme-treated WPI samples containing dithiotreitol (DTT) at protein concentrations above 10% within 120 min using 10 unit TGase/g whey proteins [Faergemand et al, 1997].…”

Section: Infl Uence Of Rtgase On Wpi Solutionmentioning

confidence: 99%

Effect of Rosemary Transglutaminase on Yoghurt Fortified with Whey Protein Isolate

Ibrahim

Glibowski

Nour

et al. 2017

Pol. J. Food Nutr. Sci.

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Rosemary (Rosmarinus offi cinalis L.) transglutaminase (RTGase) was used to cross-link whey protein isolate (WPI) and its ability to induce gelation was investigated. The rheological and textural properties of WPI were improved with RTGase treatment. Set-type yoghurts fortifi ed with 1% WPI powder treated with RTGase at the level of 2.5 and 10 unit/g protein were studied. Chemical, rheological, textural and organoleptic properties of the yoghurt treated with RTGase were better than these of the control yoghurt.

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“…Thus the properties are thoughts to be similar, however, the enzymatic properties of these enzymes have not been clearly determined. Faergamand et al (1997) mentioned a little about the difference between TGase from S. mobaraense var. and S. lydicus but details of the enzymatic properties were not known.…”

mentioning

confidence: 99%

Comparison of Enzymatic Properties of Microbial Transglutaminase from Streptomyces sp.

Umezawa¹,

Ohtsuka²,

Yokoyama³

et al. 2002

FSTR

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The microbial transglutaminase (TGase) from Streptomyces libani was purified from its culture broth and its enzymatic properties were compared with those of TGase from Streptoverticillium mobaraense var. TGase was purified by ion-exchange chromatography and size-exclusion chromatography. The specific activity of the main component was 10.7 unit/mg protein, lower than that of Streptoverticillium mobaraense var. (25 unit/mg). Several differences of enzymatic properties were found between the two enzymes. Optimum temperature, stability and gelation activity of TGase from Streptomyces libani were lower than those of TGase from Streptoverticillium mobaraense var, while, deamidation activity was higher. In addition, the existence of some TGases with different pI were suggested.

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Enzymatic cross-linking of whey proteins by a Ca2+-independent microbial transglutaminase from Streptomyces lydicus

Cited by 95 publications

References 24 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

Effect of Rosemary Transglutaminase on Yoghurt Fortified with Whey Protein Isolate

Comparison of Enzymatic Properties of Microbial Transglutaminase from Streptomyces sp.

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