Transglutaminase-catalyzed glycosylation of natural actomyosin (NAM) using glucosamine as amine donor: Functionality and gel microstructure

Hrynets, Yuliya; Ndagijimana, Maurice; Betti, Mirko

doi:10.1016/j.foodhyd.2013.09.001

Cited by 47 publications

(36 citation statements)

References 35 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%

“…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.…”

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: Introductionmentioning

confidence: 99%

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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“…However, Hrynets et al . () observed G′ values of glycosylated samples that were lower than those of nonglycosylated samples.…”

Section: Resultsmentioning

confidence: 93%

“…Hence, changes in the denaturation of the glycated myosin tail at 58 °C could be smaller than others, explaining the slight decline of G′ observed for that system. A similar finding suggested that glycosylation could reduce the unfolding and weaken the association of myosin (Hrynets et al ., ). As a result, the present study demonstrated that glycation improved the G′ of the native PSE‐like sample.…”

Section: Resultsmentioning

confidence: 97%

Improved gelation functionalities of myofibrillar protein from pale, soft and exudative chicken breast meat by nonenzymatic glycation with glucosamine

Bian

Xue

et al. 2018

Int J of Food Sci Tech

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Summary The potential of nonenzymatic glycation of myofibrillar proteins (MPs) to improve the gelation functionalities of pale, soft and exudative (PSE‐like) chicken breast meat was investigated. MP suspensions (4 mg mL−1) obtained from both normal and PSE‐like chicken breast meat were mixed with glucosamine at a ratio of 1:6 (protein : glucosamine) in phosphate‐buffered saline (0.6 m KCl, 20 mm K2HPO4/KH2PO4, 0.02% NaN3 and pH 7.5) and incubated at 37 °C for 12 h. Untreated normal and PSE‐like MP suspensions maintained at 4 °C were used as positive and negative controls, respectively. The glycation treatment increased the surface hydrophobicity but decreased the reactive sulfhydryl contents compared to those of the control (P < 0.05), indicating that the tertiary conformation of the protein changed. Correspondingly, these glycated samples also exhibited significant improvements in gel strength and the water‐holding capacity (P < 0.05). Conclusively, nonenzymatic glycation is a potential technique to improve the properties and offer a means for effective use of PSE‐like meat.

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“…It is important to note that despite the use of TGase to catalyze the covalent attachment of GlcN to glutamine-containing peptides, it is still expected the Maillard reaction occur (Hrynets et al, 2014) and thus +TGase treatments are a mixture of peptides produced by the both Maillard and TGase-aided reactions.…”

Section: Resultsmentioning

confidence: 99%

Inhibitory activity of a Concanavalin-isolated fraction from a glucosamine-peptides reaction system against heat resistant E. coli

Hrynets

Martinez

Ndagijimana

et al. 2017

Heliyon

Self Cite

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Alcalase-derived gelatin hydrolysates were glycated with glucosamine in the presence (+) or absence (−) of transglutaminase (TGase), and their antimicrobial activities toward Escherichia coli AW 1.7 were studied. Glycation treatments were subjected to concanavalin A affinity chromatography to selectively collect the glycopeptide-enriched fractions and the changes in antimicrobial activity were determined. The minimum inhibitory concentration of glycated hydrolysates decreased by 1.2 times compared to the native hydrolysate, with no differences between (+) or (−) TGase treatments. No difference was observed in the dicarbonyl compound concentration between the two glycation methods except that 3-deoxyglucosone was greater in the TGase-mediated reaction. Concanavalin A-retentate, but not the flow-through fractions, significantly improved the antimicrobial activity, however there was no difference between +TGase and −TGase glycated treatments. Purification of the retentate fraction from fluorescent compounds did not improve its antimicrobial activity.

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Transglutaminase-catalyzed glycosylation of natural actomyosin (NAM) using glucosamine as amine donor: Functionality and gel microstructure

Cited by 47 publications

References 35 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

Improved gelation functionalities of myofibrillar protein from pale, soft and exudative chicken breast meat by nonenzymatic glycation with glucosamine

Inhibitory activity of a Concanavalin-isolated fraction from a glucosamine-peptides reaction system against heat resistant E. coli

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