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

Chun-Li Song and Xin-Huai Zhao
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Chun-Li Song: College of Food and Bioengineering, Qiqihar University, Qiqihar, P.R. China
Xin-Huai Zhao: Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin, P.R. China

Czech Journal of Food Sciences, 2016, vol. 34, issue 6, 564-569

Abstract: 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.

Keywords: milk proteins; oligosaccharide; enzyme; glycation; cross-linking; property (search for similar items in EconPapers)
Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:caa:jnlcjf:v:34:y:2016:i:6:id:423-2015-cjfs

DOI: 10.17221/423/2015-CJFS

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