2015
DOI: 10.1080/19476337.2014.988647
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Effects of caseinate deamidation on transglutaminase-induced glucosamine conjugation and cross-linking as well as properties of the treated caseinates

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Cited by 4 publications
(9 citation statements)
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“…degree of deamidation of the products). This had been observed in the past three studies using casein, soy and sunflower proteins as target substrates, which provided support to the present study. DSPI1 was generated with a reaction time of 4 h and, therefore, had lower degree of deamidation than DSPI2 with a reaction time of 10 h. Based on the speciality of TGase, glutamine residues in the proteins are the sites where TGase‐induced cross‐linking and glucosamine conjugation occur.…”
Section: Resultssupporting
confidence: 90%
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“…degree of deamidation of the products). This had been observed in the past three studies using casein, soy and sunflower proteins as target substrates, which provided support to the present study. DSPI1 was generated with a reaction time of 4 h and, therefore, had lower degree of deamidation than DSPI2 with a reaction time of 10 h. Based on the speciality of TGase, glutamine residues in the proteins are the sites where TGase‐induced cross‐linking and glucosamine conjugation occur.…”
Section: Resultssupporting
confidence: 90%
“…That is, both GC‐DSPI1 and GC‐DSPI2 would possess more reactable NH 2 than GC‐SPI. Similar results was found in a previous study using casein as the targeted protein for the HCl‐induced deamidation followed by the TGase‐induced glycation and cross‐linking . It is thus verified that SPI deamidation is applicable to control (or decrease) TGase‐induced glycation and cross‐linking.…”
Section: Resultssupporting
confidence: 89%
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