Improvement of gelling properties of porcine blood plasma using microbial transglutaminase

Saguer, E.; Fort, N.; Parés, Dolors; Toldrà, Mònica; Carrétéro, C.

doi:10.1016/j.foodchem.2005.11.050

Cited by 20 publications

(7 citation statements)

References 40 publications

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“…Furthermore, gels formed after enzymatic treatment of mixed protein systems, such as peanut protein dispersions containing casein, were firmer than control samples (Clare and others 2008). Similar observations were seen using porcine blood plasma substrates as well (Saguer and others, 2007). Therefore, as earlier discussed, the actual performance characteristics of resultant TGase processed end products may be quite different, dependent upon the specific protein substrate and exact experimental parameters used during catalysis.…”

Section: Resultssupporting

confidence: 82%

Expanded Functionality of Modified Whey Protein Dispersions after Transglutaminase Catalysis

Clare

Daubert

2011

Journal of Food Science

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The functionality of whey dispersions, prepared with a modified whey protein concentrate (mWPC) ingredient, was significantly altered after cross-linking with microbial transglutaminase (TGase) upon pH adjustment to 8. Test TGase-mWPC solutions, pH 8, gelled faster than control mWPC dispersions, as measured in real time; whereas, the gelling temperature of pretreated TGase-mWPC samples (37 °C, 2.5 h) increased from 67.8 to 74.8 °C with a minimal change in gel strength. Prolonged prior incubation with the enzyme (37 °C, 20 h) raised the gel strength in both control mWPC and TGase-mWPC dispersions, though these values were approximately 2.7 times lower in TGase-mWPC samples. Furthermore, the gelling temperature was raised by 9 °C after extensive polymerization. The water holding capacity was not impacted by enzymatic processing while emulsions prepared with TGase-mWPC dispersions proved very stable with no evidence of phase separation during storage at room temperature for 1 mo. Moreover, the apparent viscosity of TGase-mWPC emulsions exhibited a 10-fold increase compared to nonenzyme-treated mWPC samples. The particle size was nearly 11 μm in covalently linked TGase-mWPC test fractions compared with 8 μm in nonpolymerized mWPC dispersions. Ultimately, the functional characteristics of TGase-mWPC ingredients may be designed to deliver superior performance, especially with regard to improving heat and emulsion stability.

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Section: Resultssupporting

confidence: 82%

Expanded Functionality of Modified Whey Protein Dispersions after Transglutaminase Catalysis

Clare

Daubert

2011

Journal of Food Science

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“…3. Moreover, using the caffeic acid and genipin as natural cross-linkers caused aggregation as shown in the higher molecular weight remaining on stacking gel (>250 kDa), which could not be migrated due to immobilisation of the molecules through the stacking gel into a separating gel (Saguer et al, 2007;Nuthong et al, 2009a). Therefore, the addition of small amounts of rutin exhibited the highest cross-linking ability among other natural cross-linkers.…”

Section: Sds-pagementioning

confidence: 99%

“…The similar protein band intensities at around 20 and 75 kDa of modified PPP with caffeic acid (lane 5-lane 7) and modified PPP with genipin (lane 8-lane 10) might be a result of the small peptides from cross-linking. Moreover, using the caffeic acid and genipin as natural cross-linkers caused aggregation as shown in the higher molecular weight remaining on stacking gel (>250 kDa), which could not be migrated due to immobilisation of the molecules through the stacking gel into a separating gel (Saguer et al, 2007;Nuthong et al, 2009a). Phenolic compounds may interact covalently or noncovalently with proteins to form protein cross-linking and leading to the precipitation or aggregation of the proteins (Strauss & Gibson, 2004).…”

Section: Sds-pagementioning

confidence: 99%

Modification and characterisation of porcine plasma protein with natural agents as potential cross‐linkers

Samsalee

Sothornvit

2017

Int J of Food Sci Tech

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Summary Modification of porcine plasma protein (PPP) using the natural cross‐linkers at different concentrations of rutin (0.6–1% w/w), caffeic acid (1–3% w/w) and genipin (0.15–0.5% w/w) on chemical and thermal properties of PPP was investigated. Among these, rutin was the most significant effective natural agent corresponding to a decrease in the free amino group and sulphydryl group contents including a change in the protein bands’ intensity from SDS‐PAGE. However, genipin exhibited greater thermal properties of modified PPP. Moreover, the modification affected the colour of PPP and a change in the FT‐IR spectra of the samples. The suitable concentrations of each natural agent were 0.6% rutin, 0.5% genipin and 3% caffeic acid. Therefore, natural cross‐linkers such as rutin, caffeic acid and genipin can be considered as alternative cross‐linkers to improve the properties of PPP for food processing and biopolymer material applications as they are nontoxic.

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“…When amine is lacking as a substrate, TGase uses water molecules as emergency catchers to catalyze deamination of degraded glutamine. E-lysine crosslinking may be intra-or extra-molecular and may cause physical changes in protein-rich foods that particularly contain lysine and glutamine (Saguer et al, 2007). TGase may as well affect the other bonds in proteins (for instance bonds between meat and soy protein and casein and gluten, respectively).…”

Section: Introductionmentioning

confidence: 99%

A research on determination of quality characteristics of chicken burgers produced with transglutaminase supplementation

Uran

Yılmaz

2017

Food Sci. Technol

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Transglutaminases are enzymes that catalyze the cross-linking between peptides or proteins. They play an important role in heat stability, gel-formation capability, water-holding capacity, emulsification and nutritional properties of proteins. They are preferred in the use of a variety of meat products due to the binding properties. In this study the effect of transglutaminase on the quality characteristics of chicken burgers were investigated. The enzyme was added at 5 different concentrations (0.2%, 0.4%, 0.6%, 0.8% and 1%) and the other treatments applied in burger production were followed. After the product was formed, it was left in the cold for a while and then analyses were carried out. According to the results, the enzyme contribution did not cause changes in the nutritional items (ash, fat, protein) of the product groups. However, there was a significant decrease in the cooking loss and a significant increase in the texture values in the groups in which the enzyme amount was increased. Although the texture of the products have been increased, the transglutaminase treatment did not effect sensory parameters of burgers compared to the control samples. Scanning Electron Microscopy (SEM) images also supported to the texture values of samples with the increase of cross-linking in microstructure.Keywords: transglutaminase; chicken burger; quality; textural properties; microstructure.Practical Application: The transglutaminase enzyme is able to reduce cooking loss by improving the textural properties of chicken burgers.

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Improvement of gelling properties of porcine blood plasma using microbial transglutaminase

Cited by 20 publications

References 40 publications

Expanded Functionality of Modified Whey Protein Dispersions after Transglutaminase Catalysis

Expanded Functionality of Modified Whey Protein Dispersions after Transglutaminase Catalysis

Modification and characterisation of porcine plasma protein with natural agents as potential cross‐linkers

A research on determination of quality characteristics of chicken burgers produced with transglutaminase supplementation

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