The objective of the present work was to separate and identify antioxidant peptides from a simulated gastrointestinal digest (Id) from Amaranthus mantegazzianus proteins (I), which has previously been demonstrated to have this activity. I and Id were separated by preparative RP-HPLC. Fractions were evaluated by the ORAC method and the more active ones were analyzed by LC-MS/MS. Each fraction presented diverse peptides from different proteins, most of them from the 11S globulin. After grouping the peptides from 11S globulin according to their overlapping sequences, and based on previous information about structure-activity relationships, ten sequences were synthesized, in order to evaluate their antioxidant activity. Four peptides presented interesting activity: AWEEREQGSR>YLAGKPQQEH∼IYIEQGNGITGM∼TEVWDSNEQ. They exhibited some of the structural characteristics already known to demonstrate this activity, all of them containing at least one bulky aromatic residue. All belonged to little structured, internal or exposed regions of the acid subunit of the 11S globulin.
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http://dx.doi.org/10.1016/j.foodchem.2015.11.092 | DOI Listing |
J Food Sci
December 2024
School of Biology and Food Engineering, Changshu Institute of Technology, Changshu, P.R. China.
Transglutaminase (TGase)-mediated cross-linking has gained significant attention due to its potential to reduce the allergenicity of food proteins. This study investigates the effects of TGase cross-linking on allergenicity and conformational modifications in a dual-protein system comprising soy protein isolate (SPI) and β-lactoglobulin (β-LG). The results showed that TGase cross-linking effectively decreased the allergenic potential of both SPI and β-LG, with a more pronounced reduction observed in the allergenicity of soy protein in the dual-protein system.
View Article and Find Full Text PDFCarbohydr Polym
February 2025
School of Food Science and Engineering, Hainan University, Haikou 570228, China. Electronic address:
Curr Res Food Sci
November 2024
INRAE, UR BIA, F-44316, Nantes, France.
The food transition towards an increased consumption of plant proteins aimed at limiting environmental impacts requires a diversification of plant protein sources. In this study, we explored the potentialities of the sustainable oilseed crop camelina to provide dietary proteins and to prepare oil-in-water emulsions. An innovative green refinery process, including the removal by ultrasound of the mucilage attached at the surface of the seeds and extraction by grinding in water at pH 8, was used to recover aqueous extracts containing camelina seed proteins.
View Article and Find Full Text PDFUltrason Sonochem
December 2024
Department of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, No. 1, Xuehai Street, Songbei District, Harbin 150028, Heilongjiang, China. Electronic address:
This study aimed to explore the impact of varying Ca concentrations and 11S/7S ratios on the gel performance of soybean protein gels (SPGs) under ultrasonication (400 W, 15 min) and to clarify the mechanisms involved. Results showed Ca addition altered the structure of soybean 11S/7S protein gels. Low Ca levels increased the turbidity, hardness, and water retention of the gels, whereas high levels disrupted the orderly aggregation of 11S/7S proteins, creating a rough, porous network.
View Article and Find Full Text PDFBiosens Bioelectron
February 2025
Guangdong Provincial Key Laboratory of Food Quality and Safety, College of Food Science, South China Agricultural University, Guangzhou, Guangdong, 510642, China. Electronic address:
In this work, with parathion, a typical forbidden organophosphate pesticide as target drug, an enhanced nanobody-driven bioluminescent immunoassay based on the engineered split-nanoluciferase (NanoLuc) was proposed. Concretely, through labeling 11S and β10, two split-NanoLuc units onto the anti-parathion nanobody (Nb) VHH9 and the artificial antigen H1 coupled with carrier protein ovalbumin (H1-OVA) respectively, an NanoLuc Binary Technology (NanoBiT) system was firstly developed in the form of homogeneous immunoassay, in which the luminescence signal was produced by the reassembled NanoLuc after the combination of the 11S-fused VHH9 and β10-labeled H1-OVA. Subsequently, in order to enhance the signal-to-noise (S/N) ratio, a novel strategy of splitting 11S into two smaller subunits Δ11S and β9 was adopted so then an NanoLuc Ternary Technology (NanoTeT) system based on tri-part components of β9-fused VHH9, β10-labeled H1-OVA and Δ11S was successfully established.
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