Abstract
Protein isolates were recovered from scallop (Patinopecten yessoensis) gonads to develop a novel functional matrix by investigating their physiochemical and functional properties. Scallop gonad protein isolates (SGPIs) were prepared from degreased scallop gonads (DSGs) by an alkali extraction and isoelectric solubilization/precipitation (ISP) process. The protein compositions of the SGPIs were mainly vitellogenin and beta-actin with molecular weights of 266 and 42 kDa, respectively, as determined using Nano-liquid chromatography-mass/mass (Nano-LC-MS/MS). After the ISP process, the protein solubility of the SGPIs was significantly improved, and the surface hydrophobicity of SGPIs intensely increased by 1.1-fold, which were attributed to the exposure of aromatic residues such as phenylalanine, tyrosine, and tryptophan. However, the content of total/reactive sulfhydryl in SGPIs was decreased compared with that of DSGs. Meanwhile, the ISP process caused partial protein unfolding, as indicated by circular dichroism analysis, which exhibited a remarkable rise in the β-sheet content with a parallel decline in the α-helix and random coil contents (P < 0.05). SGPIs exhibited a better oil absorption capacity and foaming property than both DSGs and soybean protein isolates (SPIs). Moreover, the emulsifying capacity of SGPIs was greatly enhanced by the ISP process, which was superior to the effect of commercial SPIs and was ascribed to its favorable solubility as well as surface characteristics. Practical Application: During the processing of scallop (Patinopecten yessoensis) adductors, scallop gonad, a high-protein part, is usually discarded as processing by-products despite its edibility. In recent years, scallop gonads are regarded as good sources to develop protein matrices due to their high protein content and numerous nutrients. In this study, scallop gonad protein isolates (SGPIs) were isolated by isoelectric solubilization/precipitation (ISP) process. The preferable solubility, foaming property coupled with high emulsifying property of SGPIs indicated that the SGPIs could be potentially utilized as a good protein emulsifier and additives in production of kamaboko gels, hamburger patties, sausages, and pet foods.
Original language | English |
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Pages (from-to) | 1023-1034 |
Number of pages | 12 |
Journal | Journal of Food Science |
Volume | 84 |
Issue number | 5 |
DOIs | |
State | Published - May 2019 |
Bibliographical note
Funding Information:We thank Hang Xiao and David Julian McClements of Dept. of Food Science, Univ. of Massachusetts, Amherst, Massachusetts, USA, for the technical support. This study was supported financially by the Natl. Key R&D Program of China (no. 2018YFC0311205), the Natl. Natural Science Foundation of China (No. 31671808), and the Innovative Talent Support Program for Colleges and Universities of Liaoning Province (LR2017031).
Publisher Copyright:
© 2019 Institute of Food Technologists®
Keywords
- functional characterization
- isoelectric solubilization/precipitation
- physicochemical properties
- protein isolates
- scallop (Patinopecten yessoensis)
ASJC Scopus subject areas
- Food Science