In:
Journal of Food Science, Wiley, Vol. 86, No. 6 ( 2021-06), p. 2387-2397
Kurzfassung:
Gelation properties of myofibrillar protein (MP)/wheat gluten (WG) induced by glutamine transaminase (TGase) were studied. Results showed that the inclusion of transglutaminase increased the gel strength, water‐holding capacity (WHC), and nonfreezable water (Wnf) of MP/WG mixture. Circular dichroism (CD) analysis showed that the β‐sheet and random coil content of the MP/WG treated with TGase addition increased by 12.1% and 3.7%, while the α‐helix and β‐turn content decreased by 14.2% and 1.8%. Rheological measurements showed that TGase induced higher energy storage modulus value during the MP/WG gel heating‐cooling cycle. the hydrogen bond and hydrophobic interaction content of the MP/WG gels increased by 80 and 120 ug/L, and the disulfide bond decreased by 200 ug/L, with TGase addition was increased from 0 to 120 U/g protein. Scanning electron microscope (SEM) showed that MP/WG gel with TGase had uniform and dense network structure. Practical Application The properties of myofibrillar/wheat gluten gel induced by TGase crosslinking was studied. The gel structure and water holding capacity of MP/WG were improved by the cross‐linking of TGase. The study of the gel properties of MP/WG induced by TGase crosslinking also can provide a theoretical basis for analyzing the effect of TGase on the application of gluten protein in complex meat emulsion system.
Materialart:
Online-Ressource
ISSN:
0022-1147
,
1750-3841
DOI:
10.1111/1750-3841.15774
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2021
ZDB Id:
2006705-7
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