Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product

Jiang, Shujuan; Zhao, Xin‐Huai

doi:10.1016/j.idairyj.2010.12.004

Cited by 72 publications

(72 citation statements)

References 37 publications

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“…TGase-induced glucosamine glycation could improve the solubility of actomyosin (Hrynets et al, 2014) and caseinate (Jiang & Zhao, 2011). Similarly, the present evaluation also showed that GC-CN had better solubility than caseinate (Figure 2).…”

Section: Effects Of Deamidation On Functional Properties Of the Obtaisupporting

confidence: 74%

“…Glucosamine conjugation and cross-linking of DCN1 and DCN2 as well as the following treatments were carried out as per the study of Jiang and Zhao (2011), but a higher protein concentration (50 g/L) was used in preparation. The molar ratio of glucosamine acceptor to acyl donor was also fixed at 3:1.…”

Section: Preparation Of Glucosamine-conjugated and Cross-linked Deamimentioning

confidence: 99%

“…TGase has been widely used in many studies to treat proteins, resulting in modified solubility (Di Pierro et al, 2007), emulsifying properties (Hrynets, Ndagijimana, & Betti, 2014), gelation (Zhang et al, 2014), and other properties. In a recent study, Jiang and Zhao (2011) proposed a new application of TGase: conjugating glucosamine (a monosaccharide having amino groups) into caseinate using TGase as biocatalyst. Their evaluation results showed that the obtained product contained glucosamine (i.e., it was a glycoprotein) and exhibited better interfacial stability, enhanced rheological properties, and lower surface hydrophobicity than original caseinate and a TGase cross-linked caseinate.…”

Section: Introductionmentioning

confidence: 99%

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Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

Yao¹,

Zhao²

2015

CyTA - Journal of Food

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Section: Effects Of Deamidation On Functional Properties Of the Obtaisupporting

confidence: 74%

Section: Preparation Of Glucosamine-conjugated and Cross-linked Deamimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

Yao¹,

Zhao²

2015

CyTA - Journal of Food

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“…It has been found that protein unfolding and exposure of hydrophobic residues previously buried in tertiary structure during cross-linking will bring about enhanced surface hydrophobicity (Hiller & Lorenzen, 2008). Two past studies have found that the glycated and cross-linked protein products from caseinate and soybean protein have lower surface hydrophobicity than caseinate and soybean protein (Jiang & Zhao, 2011;Song & Zhao, 2014), and thus share inconsistent results with the present study.…”

Section: Properties Of the Gc-spicontrasting

confidence: 80%

“…Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis was carried out as per the method of Jiang and Zhao (2011), by using running and stacking gels of 120 and 40 g/L, respectively. The gels were stained by Coomassie Brilliant Blue R250 of 25 g/L and the pararosaniline-Schiff reagent to detect protein and saccharide fractions, respectively.…”

Section: Chemical and Electrophoretic Analysesmentioning

confidence: 99%

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

Zhu

Liu

et al. 2015

CyTA - Journal of Food

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Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan Cambios en la estructura y en las propiedades del aislado de proteína de soja como resultado de la glicación y reticulación mediante transglutaminasa y chitosán degradado A glycated and cross-linked soybean protein isolate (GC-SPI) with the glucosamine content of 19.40 g/kg protein was prepared by using SPI, transglutaminase, and a degraded chitosan under fixed conditions, aiming to assess modified properties and potential application of GC-SPI. GC-SPI has less reactable -NH 2 groups than SPI (0.38 versus 0.48 mol/kg protein), and is verified by electrophoretic analysis to be a glycated and cross-linked protein product. Infrared spectroscopy and circular dichroism analyses demonstrate that GC-SPI contains more -OH groups, and has a more open secondary structure. In comparison with SPI, GC-SPI has higher surface hydrophobicity but lower in vitro digestibility due to protein cross-linking, and exhibits greater water-and oil-binding capacities (9.9 versus 6.4 and 3.7 versus 2.0 kg/kg protein). It is concluded that the glycation and cross-linking confer an open structure and modified properties of SPI, and GC-SPI is a potential ingredient with better hydration and oil-binding than SPI.Keywords: soybean protein isolate; degraded chitosan; transglutaminase; secondary structure; property Se preparó aislado de proteína de soja glicada y reticulada (GC-SPI) con un contenido de glucosamina de 19,40 g/kg de proteína utilizando SPI, transglutaminasa y chitosán degradado sometido a condiciones determinadas con el objetivo de estudiar las propiedades modificadas y las aplicaciones potenciales de GC-SPI. GC-SPI obtuvo menos grupos reactivos de tipo NH 2 en comparación con SPI (0,38 frente a 0,48 mol/kg de proteína) y se verificó mediante análisis electroforético para ser un producto proteínico glicado y reticulado. La espectroscopía infrarroja y el análisis de dicroísmo circular mostraron que el GC-SPI contiene más grupos OH y tiene una estructura secundaria más abierta. En comparación con SPI, GC-SPI tiene una mayor superficie de hidrofobia aunque una menor digestibilidad in vitro debido a la reticulación proteínica, además exhibe una mayor capacidad de retención de agua y de aceite (9,9 frente a 6,4 y 3,7 frente a 2,0 kg/kg de proteína). En conclusión, la glicación y la reticulación conceden una estructura abierta y unas propiedades modificadas en SPI. Además GC-SPI se trata de un ingrediente potencial con una mejor hidratación y capacidad de retención que SPI.Palabras clave: aislado de proteína de soja; chitosán degradado; transglutaminasa; estructura secundaria; propiedad

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Green synthesis of glyco‐phenol by enzymatic coupling between ferulic acid and glucosamine: An ecofriendly procedure

Aljawish

Chevalot

Paris

et al. 2021

Biotech and App Biochem

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A new glyco‐phenol was produced by the coupling between glucosamine (Glu) and ferulic acid (FA) using Myceliophthora thermophila laccase as biocatalyst in mild conditions (distilled water and 30°C) as an environmentally friendly process. Results indicated that the enzymatic reaction created a new derivative (FA–Glu), produced from coupling between Glu and FA by covalent bonds. By the high production of (FA–Glu) derivative and its stability, the optimal ratio of (FA:Glu) was of (1:1) at optimal time reaction of 6 h. Under these optimal conditions, almost 55% of ‐NH2 groups on Glu were bound with FA oxidation products. The new derivative showed higher hydrophobic character than Glu due to the presence of FA in its structure. Liquid chromatography–mass spectrometry analysis showed that (FA–Glu) derivative exhibited a molecular mass at MM 713 g/mol containing one Glu molecule and three FA molecules after decarboxylation. Furthermore, the new derivative presented good antioxidant and antiproliferative activities in comparison with Glu and FA. These results suggest that the enzymatic conjugation between Glu and FA is a promising process to produce a new glyco‐phenol having good functional properties for potential applications.

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Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product

Cited by 72 publications

References 37 publications

Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

Green synthesis of glyco‐phenol by enzymatic coupling between ferulic acid and glucosamine: An ecofriendly procedure

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