The preparation of an oligochitosan‐glycosylated and cross‐linked caseinate obtained by a microbial transglutaminase and its functional properties

Song, Chunli; Zhao, Xin‐Huai

doi:10.1111/1471-0307.12091

Cited by 29 publications

(16 citation statements)

References 41 publications

(69 reference statements)

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“…1B revealed that only GC-caseinate other than original caseinate contained glycoprotein fractions as these protein polymers were also stained using the Pararosaniline-Schiff reagent. Thus, TGase-induced glycosylation and crosslinking of caseinate occurred, in agreement with reported results that glucosamine and oligochitosan were incorporated into caseinate with crosslinking of caseinate (11,12).…”

Section: Resultssupporting

confidence: 92%

“…The thermal stability of catalase was improved based on TGase-induced incorporation of aminated β-cyclodextrin (9), and the gel strength of gelatin was enhanced using TGase in the presence of chitosan (10). Based on TGase-induced glycosylation, the 2 amino-containing saccharides glucosamine and oligochitosan were incorporated into caseinate (11,12), resulting in products with better water-binding and, especially, enhanced rheological properties. However, incorporation of other amino-containing saccharides into food proteins and the resulting properties of products also need detailed investigation.…”

Section: Introductionmentioning

confidence: 99%

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Property modification of caseinate responsible to transglutaminase-induced glycosylation and crosslinking in the presence of a degraded chitosan

Zhu

Wang

Zhao

2015

Food Sci Biotechnol

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Transglutaminase at a concentration of 10 kU/kg of protein and degraded chitosan were used for glycosylation and crosslinking of caseinate at a fixed molar ratio of the acyl acceptor to the acyl donor of 3:1, a protein concentration of 50 g/L, a pH 7.5 at 37 o C, and a reaction time of 4 h. Electrophoretic and chemical analyses showed glycosylation and crosslinking of caseinate. Glycosylated and crosslinked caseinate (GC-caseinate) contained glucosamine at 12.77 g/kg of protein, and the protein fraction had fewer reactable amino groups than original caseinate (0.58 vs. 0.64 mol/kg of protein). GC-caseinate exhibited an enhanced surface hydrophobicity, in vitro digestibility, water-binding capacity, and rheological properties, with poor protein dispensability and emulsification activity, but a similar oilbinding capacity and emulsion stability, compared with original caseinate. GC-caseinate also exhibited better properties than transglutaminase-crosslinked caseinate. Glycosylation and crosslinking was effective for better water-binding and rheological properties of caseinate.

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Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Property modification of caseinate responsible to transglutaminase-induced glycosylation and crosslinking in the presence of a degraded chitosan

Zhu

Wang

Zhao

2015

Food Sci Biotechnol

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“…This result proves an indirect fact: the oligochitosan of 1 kDa was covalently linked to the molecules of caseinate during the reaction. This result is supported by a previous result of HPLC analysis (Song & Zhao 2014a), in which only GC-caseinate (but neither caseinate nor cross-linked caseinate) was detected to have conjugated glucosamine at a level of 4.74 g/kg protein.…”

Section: Resultssupporting

confidence: 84%

“…GC-caseinate was prepared as previously described (Song & Zhao 2014a). The acidified gels were prepared as per the Koh et al (2002) method with minor modifications.…”

Section: Methodsmentioning

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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“…Evaluation of functional properties. Surface hydrophobicity of sunflower 11S globulin and its hydrolysates was measured according to the method of (Song & Zhao 2014) using 1-anilino-8-naphthalene sulphonate (ANS) as a probe. The sample solution was diluted to obtain various concentrations (0.025-0.4 g/l) by the phosphate buffer, and was thoroughly mixed with 25 μl 8 mmol/l ANS (10 mM phosphate buffer, pH 7.0).…”

Section: Methodsmentioning

confidence: 99%

Modification of structural and functional properties of sunflower 11S globulin hydrolysates

Ren¹,

Song²,

Wang³

et al. 2015

Czech J. Food Sci.

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Ren J., Song Ch.-L., Wang P., Li S., Kopparapu N.-K., Zheng X.-Q. (2015): Modification of structural and functional properties of sunflower 11S globulin hydrolysates. Czech J. Food Sci., 33: 474-478.The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

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The preparation of an oligochitosan‐glycosylated and cross‐linked caseinate obtained by a microbial transglutaminase and its functional properties

Cited by 29 publications

References 41 publications

Property modification of caseinate responsible to transglutaminase-induced glycosylation and crosslinking in the presence of a degraded chitosan

Property modification of caseinate responsible to transglutaminase-induced glycosylation and crosslinking in the presence of a degraded chitosan

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

Modification of structural and functional properties of sunflower 11S globulin hydrolysates

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