Wei-Cai Zeng
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Wei-Cai Zeng has a total of 124 co-authors. Here are the top co-authors by number of shared publications:
Nan Chen
38 shared publicationsQiang He
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu 610065, PR China
32 shared publicationsQian-Da Xu
20 shared publicationsQun Sun
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu 610065, PR China
15 shared publications- Qiang He
College of Biomass Science and Engineering, Sichuan University, Chengdu 610065, PR China
11 shared publications Hao-Xiang Gao
School of Food and Strategic Reserves, Henan University of Technology, Zhengzhou, 450001, PR China
10 shared publications
Latest Publications
- Open Access
- 20 February 2026
- Published by Elsevier in Food Chemistry: X
- Vol. 34
Potential of tea polyphenols to ameliorate the quality of beef meatballs during frozen storage and its action mechanism
- 20 February 2026
- Published by Elsevier in Food Chemistry: X
- Vol. 34
Open AccessPotential of tea polyphenols to ameliorate the quality of beef meatballs during frozen storage and its action mechanism
- 16 February 2026
- Published by Elsevier in Food Chemistry
- Vol. 508 (Pt B) , 148466
Modulation of protein self-assembly via hydrolysis and metal ion coordination: Effects on EGCG encapsulation and controlled release
- 16 February 2026
- Published by Elsevier in Food Chemistry
- Vol. 508 (Pt B) , 148466
Modulation of protein self-assembly via hydrolysis and metal ion coordination: Effects on EGCG encapsulation and controlled release
- 15 January 2026
- Published by Wiley in Journal of Food Science
- Vol. 91 (1) , e70866
Regulation of Tea Polyphenols on the Gel Properties of Soy Protein and the Action Mechanism
Effects of non‐covalent interactions between tea polyphenols (TPs) and soybean protein isolate (SPI) on the structural and functional properties of soy protein gels were investigated, and the potential action mechanism was further explored. SPI was firstly non‐covalent bound with TP to form the SPI–TP gel, and its structural characteristics, physicochemical properties, rheological properties, and digestion properties were determined. TP exhibited the strong capability to form hydrogen bonds and/or hydrophobic interactions with SPI, which was concentration‐dependent. Moderate addition of TP could effectively regulate the strength of different interactions in gel, such as interactions of proteins and interactions between proteins and water molecules, thereby yielding gels with good gel strength and hydration capacity. With increase of addition concentration, TP showed the capability to induce protein structural unfolding and formed new non‐covalent interactions with proteins, which facilitated the formation of a more robust and uniform gel network, thereby improving gel's properties. However, excessive addition of TP caused the excessive cross‐linking of protein, ultimately compromising gel strength and structural stability. Additionally, during in vitro digestion, the addition of TP reduced the digestion of protein in gel but significantly enhanced the antioxidant properties of the digesta. All results suggest that TPs have the potential to effectively regulate the structure and function of SPI gels, which provides the theoretical guidance and research foundations for the application of protein–polyphenol complexes as functional food ingredients or biomaterials in food and chemical industries.
- 15 January 2026
- Published by Wiley in Journal of Food Science
- Vol. 91 (1) , e70866
Regulation of Tea Polyphenols on the Gel Properties of Soy Protein and the Action Mechanism
Effects of non‐covalent interactions between tea polyphenols (TPs) and soybean protein isolate (SPI) on the structural and functional properties of soy protein gels were investigated, and the potential action mechanism was further explored. SPI was firstly non‐covalent bound with TP to form the SPI–TP gel, and its structural characteristics, physicochemical properties, rheological properties, and digestion properties were determined. TP exhibited the strong capability to form hydrogen bonds and/or hydrophobic interactions with SPI, which was concentration‐dependent. Moderate addition of TP could effectively regulate the strength of different interactions in gel, such as interactions of proteins and interactions between proteins and water molecules, thereby yielding gels with good gel strength and hydration capacity. With increase of addition concentration, TP showed the capability to induce protein structural unfolding and formed new non‐covalent interactions with proteins, which facilitated the formation of a more robust and uniform gel network, thereby improving gel's properties. However, excessive addition of TP caused the excessive cross‐linking of protein, ultimately compromising gel strength and structural stability. Additionally, during in vitro digestion, the addition of TP reduced the digestion of protein in gel but significantly enhanced the antioxidant properties of the digesta. All results suggest that TPs have the potential to effectively regulate the structure and function of SPI gels, which provides the theoretical guidance and research foundations for the application of protein–polyphenol complexes as functional food ingredients or biomaterials in food and chemical industries.
- 12 December 2025
- Published by Springer Nature in Journal of Food Measurement and Characterization
- Vol. 20 (3) , 3000-3012
Effects of protein characteristics on three methods for determination of total phenolic content in food systems
- 12 December 2025
- Published by Springer Nature in Journal of Food Measurement and Characterization
- Vol. 20 (3) , 3000-3012
Effects of protein characteristics on three methods for determination of total phenolic content in food systems
- 18 November 2025
- Published by Elsevier in Food Research International
- Vol. 223 (Pt 2) , 117848
Dual protein-cyclodextrin carriers regulated by metal ions and tannic acid for encapsulation and functional protection of lycopene
- 18 November 2025
- Published by Elsevier in Food Research International
- Vol. 223 (Pt 2) , 117848
Dual protein-cyclodextrin carriers regulated by metal ions and tannic acid for encapsulation and functional protection of lycopene
- Open Access
- 18 October 2025
- Published by Elsevier in Food Chemistry: X
- Vol. 31
Effect of metal types on the controllable supramolecular self-assembly of protein-polyphenol conjugates and their carrier capabilities
- 18 October 2025
- Published by Elsevier in Food Chemistry: X
- Vol. 31
Open AccessEffect of metal types on the controllable supramolecular self-assembly of protein-polyphenol conjugates and their carrier capabilities
- Open Access
The Effect of Longan Peel and Seed on Wheat Starch and the Quality of Longan Cake
In the present study, the effects of longan peel and seed on the quality of longan cake were determined, and the effects of longan peel extract (LPE) and longan seed extract (LSE) on the physicochemical properties of wheat starch were also measured. Furthermore, the phenolic profile and antioxidant activities of these extracts were observed. The results showed that both longan peel and seed could improve the color, texture, and volatile flavor compounds of longan cake. In addition, the properties of wheat starch, including gelatinization characteristics, thermogravimetric analysis, rheological properties, solubility, swelling power, water/oil-holding capacity and iodine binding ability, were all affected by LPE and LSE significantly. Both LPE and LSE had high contents of total phenols (LPE: 71.05 ± 2.57 mg/g, LSE: 78.49 ± 5.21 mg/g) and total flavonoids (LPE: 286.27 ± 6.04 mg/g, LSE: 423.21 ± 7.69 mg/g). Gallic acid, ellagic acid, and ellagic acid 4-O-α-l-arabinofuranoside were identified as the main phenolic compounds of LPE, while those of LSE were gallic acid, ellagic acid, ellagic acid 4-O-α-l-arabinofuranoside and (-)-epicatechin. Furthermore, LPE and LSE both exhibited good antioxidant activities to scavenge free radicals and showed high reducing power. All results suggest that longan peel and seed are rich in phenols and can improve the properties of starch so as to enhance the quality of starch product, which shows their potential application in food and chemical industries.
Open AccessThe Effect of Longan Peel and Seed on Wheat Starch and the Quality of Longan Cake
In the present study, the effects of longan peel and seed on the quality of longan cake were determined, and the effects of longan peel extract (LPE) and longan seed extract (LSE) on the physicochemical properties of wheat starch were also measured. Furthermore, the phenolic profile and antioxidant activities of these extracts were observed. The results showed that both longan peel and seed could improve the color, texture, and volatile flavor compounds of longan cake. In addition, the properties of wheat starch, including gelatinization characteristics, thermogravimetric analysis, rheological properties, solubility, swelling power, water/oil-holding capacity and iodine binding ability, were all affected by LPE and LSE significantly. Both LPE and LSE had high contents of total phenols (LPE: 71.05 ± 2.57 mg/g, LSE: 78.49 ± 5.21 mg/g) and total flavonoids (LPE: 286.27 ± 6.04 mg/g, LSE: 423.21 ± 7.69 mg/g). Gallic acid, ellagic acid, and ellagic acid 4-O-α-l-arabinofuranoside were identified as the main phenolic compounds of LPE, while those of LSE were gallic acid, ellagic acid, ellagic acid 4-O-α-l-arabinofuranoside and (-)-epicatechin. Furthermore, LPE and LSE both exhibited good antioxidant activities to scavenge free radicals and showed high reducing power. All results suggest that longan peel and seed are rich in phenols and can improve the properties of starch so as to enhance the quality of starch product, which shows their potential application in food and chemical industries.
- 3 July 2025
- Published by Elsevier in Food Hydrocolloids
- Vol. 170
Regulation of disulfide bond cleavage on the physicochemical and digestive properties of EGCG-gluten covalent complexes
- 3 July 2025
- Published by Elsevier in Food Hydrocolloids
- Vol. 170
Regulation of disulfide bond cleavage on the physicochemical and digestive properties of EGCG-gluten covalent complexes