Effect of κ-carrageenan on gelation and gel characteristics of Antarctic krill (Euphausia superba) protein isolated with isoelectric solubilization/precipitation.

Autor: Zheng H; West Virginia University, Division of Animal and Nutritional Science, P.O. Box 6108, Morgantown, WV 26506-6108, USA; Guangdong Ocean University, College of Food Science and Technology, Zhanjiang 524088, China; Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Zhanjiang 524088, China; Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, Zhanjiang 524088, China., Beamer SK; West Virginia University, Division of Animal and Nutritional Science, P.O. Box 6108, Morgantown, WV 26506-6108, USA., Matak KE; West Virginia University, Division of Animal and Nutritional Science, P.O. Box 6108, Morgantown, WV 26506-6108, USA., Jaczynski J; West Virginia University, Division of Animal and Nutritional Science, P.O. Box 6108, Morgantown, WV 26506-6108, USA. Electronic address: jacek.jaczynski@mail.wvu.edu.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2019 Apr 25; Vol. 278, pp. 644-652. Date of Electronic Publication: 2018 Nov 28.
DOI: 10.1016/j.foodchem.2018.11.080
Abstrakt: Isoelectric solubilization/precipitation (ISP) was used to extract krill protein isolate (KPI). Due to krill endogenous proteases ISP-KPI barely forms gel which is a major hurdle in wide application of this tremendous protein source for direct human consumption. The objective was to improve gelation and elucidate interaction mechanism between κ-carrageenan and KPI. κ-Carrageenan was added to KPI at 0.00, 0.75, 1.50, 2.25, and 3.00 g/150 g and heated at 90 °C for 15 min. Added κ-carrageenan improved texture of KPI gels. However, the level of addition had minimal effect. SDS-PAGE revealed severe proteolysis of KPI even during heating. Total and free sulfhydryl were not different, while surface hydrophobicity and water-holding-capacity slightly decreased and increased, respectively with added κ-carrageenan. Fourier-transform-infrared-spectroscopy showed none-to-minimal shift of β-sheet and α-helical protein structure; while CC and CO stretching as well as CH bending of κ-carrageenan showed the greatest shift, indicating that κ-carrageenan was mainly responsible for gel formation.
(Copyright © 2018 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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