Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel

Færgemand, M.; Qvist, K.B.

doi:10.1016/s0268-005x(97)80058-6

Cited by 89 publications

(50 citation statements)

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“…Transglutaminase (TGase) can induce interaction through inter-and intra-molecular bonds in the protein molecules, resulting in formation of high molecular weight protein polymers and modification of the properties of the proteins and food products containing them (Nielsen et al 1995;Motoki and Seguro 1998). TGase had been applied in some dairy products including yoghurt (Faergemand and Qvist 1997;Lorenzen, et al 2002), but a need exists to study other enzyme systems capable of improving the quality of dairy products. Horseradish peroxidase (HRP, EC 1.11.1.7), a heme-containing enzyme from the tissue of edible horseradish (Yuan and Jiang 2003), can induce cross-linking of the proteins in the presence of H 2 O 2 and a low molecular weight hydrogen donor (e.g.…”

Section: Introductionmentioning

confidence: 99%

Quality indices of the set-yoghurt prepared from bovine milk treated with horseradish peroxidase

2012

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Horseradish peroxidase (HRP, EC 1.11.1.7) was applied to treat whole bovine milk in the presence or absence of ferulic acid (FA). The treated milk exhibited different rheological properties from the control milk, and was used to prepare set-yoghurt with commercial direct vat set starter. Some chemical, textural and rheological properties of the yoghurt prepared were measured and compared. Compared to that prepared with the control milk, the yoghurt prepared with the HRP-or HRP and FA-treated bovine milk exhibited an increased hardness and adhesiveness, lower syneresis extent, higher apparent viscosity, and higher storage modulus and viscous modulus. Observation of the microstructure of the yoghurt samples under scanning electron microscopy illustrated that HRP treatment of bovine milk led to the prepared yoghurt a more compact and uniform structure. The results in the present work stated that treatment of bovine milk with HRP in the presence of ferulic acid could be applied to improve the quality of set-yoghurt.

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Section: Introductionmentioning

confidence: 99%

Quality indices of the set-yoghurt prepared from bovine milk treated with horseradish peroxidase

2012

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“…TGase has been proved as a potential ingredient in yoghurt production for quality improvement (Gauche, Tomazi, Barreto, Ogliari, & Bordignon-Luiz, 2009). TGase treatment of milk proteins before yoghurt fermentation has other beneficial effects on yoghurt quality, such as increasing gel hardness (Faergemand & Qvist, 1997;Gauche et al, 2009), decreasing syneresis (Şanlı, Sezgin, Deveci, Şenel, & Benli, 2011), and enhancing viscosity (Ozer, Kirmaci, Oztekin, Hayaloglu, & Atamer, 2007) and elastic modulus (Anema, Lauber, Lee, Henle, & Klostermeyer, 2005). Cross-linking of milk proteins by TGase prior to yoghurt fermentation can also improve gel structure (i.e.…”

Section: Introductionmentioning

confidence: 99%

“…Cross-linking of milk proteins by TGase prior to yoghurt fermentation can also improve gel structure (i.e. protein network) of set-style yoghurt (Faergemand & Qvist, 1997;Farnsworth, Li, Hendricks, & Guo, 2006).…”

Section: Introductionmentioning

confidence: 99%

Quality attributes of the set-style skimmed yoghurt containing enzymatic cross-linked or thermal polymerized whey protein isolate

Song

Zhao

2016

CyTA - Journal of Food

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Impacts of replacing of milk proteins with two modified whey protein isolates (WPIs) on quality of set-style skimmed yoghurt were assessed. WPI dispersion (35 g protein/kg) was cross-linked by transglutaminase for 5-10 min or polymerized at 90°C or 100°C for 10-30 min, mixed with skimmed milk (35 g protein/kg) at 1:2 (v/v), and fermented by a commercial starter at 42°C for 5 h. Compared with the control yoghurt generated from skimmed milk only, these yoghurt samples showed no difference in main chemical compositions, but using the cross-linked WPI somewhat delayed yoghurt fermentation. These yoghurt samples had enhanced values of hardness, adhesiveness, springiness, and cohesiveness but decreased syneresis, especially using long-time and high-temperature treatment for WPI. The cross-linked and polymerized WPIs both conferred yoghurt samples with enhanced viscosity, elastic and viscous moduli, and finer microstructure. In general, the polymerized WPI was better than the cross-linked WPI to enhance these quality attributes.Atributos cualitativos del yogur desnatado preparado con aislado proteínico de lactosuero con reticulación encimática o polimerizado térmico RESUMEN Se evaluaron los impactos de remplazar las proteínas de la leche por dos aislados proteínicos de lactosuero modificados (WPI) en la calidad del yogur desnatado preparado. La dispersión de WPI (35 g de proteína/kg) fue reticulada mediante transglutaminasa durante 5-10 min o polimerizada a 90°C o 100°C durante 10-30 min, mezclada con leche desnatada (35 g de proteína/kg) a 1:2 (v/v), además de fermentada mediante un iniciador comercial a 42°C durante 5 h. En comparación con el yogur control generado únicamente a partir de leche desnatada, estas muestras de yogur no mostraron diferencias en las composiciones principales, aunque la utilización de WPI reticulado de alguna forma retrasó la fermentación del yogur. Estas muestras de yogur han mejorado los valores de dureza, adhesión, ligereza y cohesión, aunque también han disminuido la sinéresis, especialmente con la utilización del tratamiento a alta temperatura y larga duración de WPI. Los dos WPI reticulados y polimerizados han creado muestras de yogur con una viscosidad, elasticidad y módulos viscosos mejorados, además de una mejor estructura. En general, el WPI polimerizado fue mejor que el WPI reticulado para mejorar estos atributos cualitativos. ARTICLE HISTORY

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“…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%

“…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).…”

mentioning

confidence: 99%

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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Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel

Cited by 89 publications

References 19 publications

Quality indices of the set-yoghurt prepared from bovine milk treated with horseradish peroxidase

Quality indices of the set-yoghurt prepared from bovine milk treated with horseradish peroxidase

Quality attributes of the set-style skimmed yoghurt containing enzymatic cross-linked or thermal polymerized whey protein isolate

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

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