Effects of calcium-catechin complex core-shell microparticles on quality of surimi gel

doi:10.3969/j.issn.1004-1524.20250256

Acta Agriculturae Zhejiangensis ›› 2026, Vol. 38 ›› Issue (3): 568-580.DOI: 10.3969/j.issn.1004-1524.20250256

• Food Science • Previous Articles Next Articles

Effects of calcium-catechin complex core-shell microparticles on quality of surimi gel

WU Xiaoli¹(), CHEN Yin¹, HU Jun², CHEN Wenxuan², WEN Zhengshun³^,^*(), ZHANG Jin²^,^*()

^1. Food and Pharmacy College, Zhejiang Ocean University, Zhoushan 316022, Zhejiang, China
^2. Institute of Food Science, State Key Laboratory for Quality and Safety of Agro-Products, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, China
^3. Xianghu Laboratory, Hangzhou 311203, China

Received:2025-03-28 Online:2026-03-25 Published:2026-04-17
Contact: WEN Zhengshun,ZHANG Jin

Abstract

Abstract:

In this study, we investigated the effects of calcium-catechin complex (Ca@catechin) core-shell microparticles on the quality of surimi gel, by systematically examining their impacts on the water holding capacity, gel strength, rheological properties, secondary structure, chemical interactions and microstructure of surimi gel. The results demonstrated that the incorporation of Ca@catechin core-shell microparticles induced the formation of a more compact network structure inside the surimi gel; the gel strength was significantly (p<0.05) increased by 82.2%, and the elasticity and cohesiveness were remarkably enhanced. Fourier-transform infrared spectroscopy (FTIR) analysis revealed that Ca@catechin core-shell microparticles altered the secondary structure of surimi gel, with a decreased content of α helix and an increased content of β sheet. Such structural changes promoted the formation of hydrogen bonds in surimi gel, strengthened the cross-linking degree of disulfide bonds, and significantly reduced the total sulfhydryl content. Dynamic rheological measurements showed that the addition of Ca@catechin core-shell microparticles significantly enhanced the storage modulus (G') of surimi gel, and significantly decreased their solubility and surface hydrophobicity. In conclusion, the preparation of surimi gel with Ca@catechin core-shell microparticles can improve the functional properties and quality of surimi gel. The findings of this study lay a theoretical foundation for protein gel modification and provide scientific guidance for upgrading the quality of surimi gel products.

Key words: calcium-catechin complex core-shell microparticles, surimi, gel properties, microstructure

CLC Number:

TS254.1

WU Xiaoli, CHEN Yin, HU Jun, CHEN Wenxuan, WEN Zhengshun, ZHANG Jin. Effects of calcium-catechin complex core-shell microparticles on quality of surimi gel[J]. Acta Agriculturae Zhejiangensis, 2026, 38(3): 568-580.

Figures/Tables 12

Fig.1 Fourier transform infrared absorption spectra of different samples (A), as well as the particle size distribution (B) and scanning electron microscopy (SEM) image (C) of Ca@catechin core-shell microparticles

Table 1 Effect of different treatments on the texture of surimi gels

样品 Sample	硬度/N Hardness/N	弹性/mm Springiness/mm	胶着性/N Gumminess/N	咀嚼性/mJ Chewiness/mJ	回复性 Resilience
CK	7.95±1.62 c	2.05±0.39 c	5.37±0.45 c	10.97±0.18 c	0.72±0.08 b
ST	10.78±0.45 a	1.97±0.19 c	6.47±0.55 ab	12.79±0.16 b	0.60±0.05 c
SCA	10.40±0.32 ab	2.18±0.16 b	7.09±0.92 a	15.40±0.16 a	0.73±0.04 b
STCA	9.33±0.44 b	2.31±1.41 b	5.60±0.18 b	12.22±0.43 b	0.69±0.02 b
SCAT	7.74±1.26 c	2.53±0.12 a	6.08±0.85 ab	15.47±0.16 a	0.79±0.04 a

Fig.2 Effect of different treatments on gel strength of surimi gels Bars marked without identical letters indicate significant difference at p<0.05. The same applies to Fig. 4-7.

Fig.3 Effect of different treatments on storage modulus (G') of surimi gels

Fig.4 Effects of different treatments on protein solubility of surimi gel

Fig.5 Effect of different treatments on water holding capacity of surimi gels

Fig.6 Effect of different treatments on surface hydrophobicity of surimi gels

Fig.7 Effect of different treatments on total sulfhydryl content of surimi gels

Fig.8 Effect of different treatments on intermolecular forces of surimi gels Bars marked without identical letters indicate significant difference at p<0.05 within treatments on the same intermolecular force.

Table 2 Effect of different treatments on color and whiteness of surimi gels

样品Sample	L^*	a^*	b^*	W
CK	71.54±0.78 b	-2.18±0.14 c	5.81±0.45 c	70.87±0.76 b
ST	71.75±0.94 b	0.74±0.13 b	7.70±0.27 a	71.26±0.89 b
SCA	76.81±1.12 a	-2.12±0.14 c	5.21±0.19 c	75.48±1.12 a
STCA	72.39±0.34 b	-0.20±0.06 b	4.01±0.18 d	72.10±0.35 b
SCAT	63.37±1.07 c	2.31±0.18 a	6.41±0.85 b	62.74±1.08 c

Fig.9 Fourier transform infrared spectra (A) and secondary structure contents (B) of surimi gels under different treatments

Fig.10 Microscopic morphology of surimi gels under different treatments

References 45

[1]	MONTO A R, LI M Z, WANG X, et al. Recent developments in maintaining gel properties of surimi products under reduced salt conditions and use of additives[J]. Critical Reviews in Food Science and Nutrition, 2022, 62(30): 8518-8533.
[2]	ZHANG S J, ZHANG L Z, YIN T, et al. Exploring the versatility of carbohydrates in surimi and surimi products: novel applications and future perspectives[J]. Journal of the Science of Food and Agriculture, 2024, 104(4): 1874-1883.
[3]	AMIRI S, REZAZADEH-BARI M, ALIZADEH-KHALEDABAD M, et al. New formulation of vitamin C encapsulation by nanoliposomes: production and evaluation of particle size, stability and control release[J]. Food Science and Biotechnology, 2019, 28(2): 423-432.
[4]	PENG Y R, MENG Q L, ZHOU J, et al. Nanoemulsion delivery system of tea polyphenols enhanced the bioavailability of catechins in rats[J]. Food Chemistry, 2018, 242: 527-532.
[5]	孙媛媛, 朱绪春, 刘红芝, 等. 植物多酚调控食源蛋白结构、功能及生物特性的研究进展[J]. 食品工业科技, 2025, 46(8): 1-8.
	SUN Y Y, ZHU X C, LIU H Z, et al. Research progress on plant polyphenols regulating the structure, function, and biological characteristics of dietary proteins[J]. Science and Technology of Food Industry, 2025, 46(8): 1-8.
[6]	SHI M, HUANG L Y, NIE N, et al. Binding of tea catechins to rice bran protein isolate: interaction and protective effect during in vitro digestion[J]. Food Research International, 2017, 93: 1-7.
[7]	AMIRI S, REZAZAD BARI L, MALEKZADEH S, et al. Effect of Aloe vera gel-based active coating incorporated with catechin nanoemulsion and calcium chloride on postharvest quality of fresh strawberry fruit[J]. Journal of Food Processing and Preservation, 2022, 46(10): e15960.
[8]	HO S, THOO Y Y, YOUNG D J, et al. Inclusion complexation of catechin by β-cyclodextrins: characterization and storage stability[J]. LWT, 2017, 86: 555-565.
[9]	XIAO Y Q, KANG S F, LIU Y N, et al. Effect and mechanism of calcium ions on the gelation properties of cellulose nanocrystals-whey protein isolate composite gels[J]. Food Hydrocolloids, 2021, 111: 106401.
[10]	CHENG J R, ZHU M J, LIU X M. Insight into the conformational and functional properties of myofibrillar protein modified by mulberry polyphenols[J]. Food Chemistry, 2020, 308: 125592.
[11]	ZHAN J Q, CHEN Y W, LI G S, et al. Study on the structure and preservation mechanism of 3D-printed surimi with Ca²⁺ and xylo-oligosaccharides[J]. Food Bioscience, 2023, 54: 102905.
[12]	ZHANG S N, MURRAY B S, SURIYACHAY N, et al. Synergistic interactions of plant protein microgels and cellulose nanocrystals at the interface and their inhibition of the gastric digestion of Pickering emulsions[J]. Langmuir, 2021, 37(2): 827-840.
[13]	马海燕, 林辅坤, 雒国清, 等. 激光粒度仪在测定钽粉粒度分布中的应用[J]. 宁夏工程技术, 2017, 16(3): 260-262.
	MA H Y, LIN F K, LUO G Q, et al. Particle size distribution detection of tantalum powder by laser particle size analyzer mastersizer 2000[J]. Ningxia Engineering Technology, 2017, 16(3): 260-262.
[14]	ZHANG S S, DUAN J Y, ZHANG T T, et al. Effect of compound dietary fiber of soybean hulls on the gel properties of myofibrillar protein and its mechanism in recombinant meat products[J]. Frontiers in Nutrition, 2023, 10: 1129514.
[15]	DING J J, ZHAO X Y, LI X X, et al. Effects of different recovered sarcoplasmic proteins on the gel performance, water distribution and network structure of silver carp surimi[J]. Food Hydrocolloids, 2022, 131: 107835.
[16]	ZHU S C, WANG Y Y, DING Y C, et al. Improved texture properties and toughening mechanisms of surimi gels by double network strategies[J]. Food Hydrocolloids, 2024, 152: 109900.
[17]	LI J L, MUNIR S, YU X Y, et al. Double-crosslinked effect of TGase and EGCG on myofibrillar proteins gel based on physicochemical properties and molecular docking[J]. Food Chemistry, 2021, 345: 128655.
[18]	LI N, ZHANG K X, DONG X H, et al. Modification of the structure and function of myofibrillar protein by structurally relevant natural phenolic compounds[J]. Food Bioscience, 2023, 53: 102676.
[19]	GAO X, XIE Y R, YIN T, et al. Effect of high intensity ultrasound on gelation properties of silver carp surimi with different salt contents[J]. Ultrasonics Sonochemistry, 2021, 70: 105326.
[20]	XIE F, ZHENG W Q, FU T T, et al. Cryoprotective effect of tamarind seed polysaccharide on grass carp surimi: characteristics, interactions, and mechanisms[J]. Food Hydrocolloids, 2024, 153: 110022.
[21]	张晋, 吴晓丽, 田雨薇, 等. 超声波辅助酶解牦牛血粉提取氯化血红素的响应面工艺优化及品质表征[J]. 浙江农业学报, 2024, 36(6): 1357-1367.
	ZHANG J, WU X L, TIAN Y W, et al. Ultrasound-assisted enzymolytic extraction of chlorohemin from yak blood powder: response surface optimization and quality characterization[J]. Acta Agriculturae Zhejiangensis, 2024, 36(6): 1357-1367.
[22]	YANG Y, LIU X Y, XUE Y, et al. The process of heat-induced gelation in Litopenaeus vannamei[J]. Food Hydrocolloids, 2020, 98: 105260.
[23]	ZHOU H L, PANDYA J K, TAN Y B, et al. Role of mucin in behavior of food-grade TiO₂ nanoparticles under simulated oral conditions[J]. Journal of Agricultural and Food Chemistry, 2019, 67(20): 5882-5890.
[24]	CAI L Y, FENG J H, CAO A L, et al. Effect of partial substitutes of NaCl on the cold-set gelation of grass carp myofibrillar protein mediated by microbial transglutaminase[J]. Food and Bioprocess Technology, 2018, 11(10): 1876-1886.
[25]	XIAO Y Q, LIU Y N, WANG Y, et al. Heat-induced whey protein isolate gels improved by cellulose nanocrystals: gelling properties and microstructure[J]. Carbohydrate Polymers, 2020, 231: 115749.
[26]	JIN X Q, QU R J, WANG Y, et al. Effect and mechanism of acid-induced soy protein isolate gels as influenced by cellulose nanocrystals and microcrystalline cellulose[J]. Foods, 2022, 11(3): 461.
[27]	ZHAO Y D, WEI G P, LI J J, et al. Comparative study on the effect of different salts on surimi gelation and gel properties[J]. Food Hydrocolloids, 2023, 144: 108982.
[28]	XU H J, ZHANG J L, ZHOU Q X, et al. Synergistic effect and mechanism of cellulose nanocrystals and calcium ion on the film-forming properties of pea protein isolate[J]. Carbohydrate Polymers, 2023, 319: 121181.
[29]	翟璐, 杨加成, 陈康, 等. 金枪鱼纳米鱼骨钙对鱼糜制品凝胶特性的影响[J]. 中国食品学报, 2022, 22(5): 180-188.
	ZHAI L, YANG J C, CHEN K, et al. Effect of tuna nanoscale fish bone calcium on gelation characteristic of surimi products[J]. Journal of Chinese Institute of Food Science and Technology, 2022, 22(5): 180-188.
[30]	CHEN X, LI X Z, YANG F J, et al. Effects and mechanism of antifreeze peptides from silver carp scales on the freeze-thaw stability of frozen surimi[J]. Food Chemistry, 2022, 396: 133717.
[31]	YUAN M, FU G, SUN Y M, et al. Biosynthesis and applications of curdlan[J]. Carbohydrate Polymers, 2021, 273: 118597.
[32]	PEYRANO F, DE LAMBALLERIE M, AVANZA M V, et al. Rheological characterization of the thermal gelation of cowpea protein isolates: effect of pretreatments with high hydrostatic pressure or calcium addition[J]. LWT, 2019, 115: 108472.
[33]	JIANG X, CHEN Q, XIAO N Y, et al. Changes in gel structure and chemical interactions of Hypophthalmichthys molitrix surimi gels: effect of setting process and different starch addition[J]. Foods, 2022, 11(1): 9.
[34]	WANG T, XU P C, CHEN Z X, et al. Mechanism of structural interplay between rice proteins and soy protein isolates to design novel protein hydrocolloids[J]. Food Hydrocolloids, 2018, 84: 361-367.
[35]	WANG J, DE FIGUEIREDO FURTADO G, MONTHEAN N, et al. CaCl₂ supplementation of hydrophobised whey proteins: assessment of protein particles and consequent emulsions[J]. International Dairy Journal, 2020, 110: 104815.
[36]	陈旭, 余璐涵, 蔡茜茜, 等. 低温冷链贮藏对鱼糜凝胶化学作用力和肌原纤维蛋白结构及功能特性的影响[J]. 食品科学, 2022, 43(23): 194-201.
	CHEN X, YU L H, CAI X X, et al. Effect of cold chain storage on chemical interactions of surimi gel and structural and functional properties of myofibrillar protein[J]. Food Science, 2022, 43(23): 194-201.
[37]	WANG X, WANG L M, YANG K, et al. Radio frequency heating improves water retention of pork myofibrillar protein gel: an analysis from water distribution and structure[J]. Food Chemistry, 2021, 350: 129265.
[38]	YU N N, XU Y S, JIANG Q X, et al. Molecular forces involved in heat-induced freshwater surimi gel: effects of various bond disrupting agents on the gel properties and protein conformation changes[J]. Food Hydrocolloids, 2017, 69: 193-201.
[39]	WANG Z Y, FENG J H, LI Q Q, et al. Effect of sodium alginate and calcium chloride on the physicochemical characteristics of shrimp (Penaeus vannamei) surimi gels[J]. Journal of Ocean University of China, 2024, 23(6): 1645-1654.
[40]	ZHAO X Y, WANG X F, ZENG L J, et al. Effects of oil-modified crosslinked/acetylated starches on silver carp surimi gel: texture properties, water mobility, microstructure, and related mechanisms[J]. Food Research International, 2022, 158: 111521.
[41]	BUAMARD N, BENJAKUL S. Improvement of gel properties of sardine (Sardinella albella) surimi using coconut husk extracts[J]. Food Hydrocolloids, 2015, 51: 146-155.
[42]	ZHAO X T, LAN Y Y, YANG K, et al. Antifouling modification of PVDF membranes via in situ mixed-charge copolymerization and TiO₂ mineralization[J]. Applied Surface Science, 2020, 525: 146564.
[43]	ZHONG Q, LI H J, DENG S Y, et al. Tannic acid-induced changes in water distribution and protein structural properties of bacon during the curing process[J]. LWT, 2021, 137: 110381.
[44]	ZHUANG X B, HAN M Y, BAI Y, et al. Insight into the mechanism of myofibrillar protein gel improved by insoluble dietary fiber[J]. Food Hydrocolloids, 2018, 74: 219-226.
[45]	DENG C Y, SHAO Y Y, XU M S, et al. Effects of metal ions on the physico-chemical, microstructural and digestion characteristics of alkali-induced egg white gel[J]. Food Hydrocolloids, 2020, 107: 105956.

Effects of calcium-catechin complex core-shell microparticles on quality of surimi gel

RichHTML

PDF (PC)

Knowledge

Abstract

Cite this article

share this article

Figures/Tables 12

References 45

Related Articles 5

Recommended Articles

Metrics

Comments

[1]	ZHAO Han, XIANG Kexin, LIU Chunju, LI Bin, LI Dajing, LI Yue, NIU Liying, YU Rui. Relationship between chemical composition, microstructure and texture of different varieties of peach fruits [J]. Acta Agriculturae Zhejiangensis, 2024, 36(12): 2705-2718.
[2]	XU Shenping, YUAN Xiuyun, ZHANG Yan, LIANG Fang, JIANG Suhua, NIU Suyan, CUI Bo. Effects of temperature and light intensity on photosynthetic physiology and axillary bud development of flower stalk in Phalaenopsis [J]. Acta Agriculturae Zhejiangensis, 2023, 35(10): 2389-2397.
[3]	XIE Fang, XIA Yingxia, SU Qiangjun, UWITUGABIYE Vestine, CHEN Zhaohe, ZHOU Gang. Observation of ultramicroscopic characteristics of three morphology of mycelium for Ophiocordyceps sinensis [J]. Acta Agriculturae Zhejiangensis, 2021, 33(5): 855-860.
[4]	YAN Wenyi, XIE Yongdong, YANG Luxi, CHEN Yan, WANG Haixia, SUN Bo, HE Zhongqun. Comparison of morphology, anatomical structure and karyotype between two Talinum crassifolium (Jacq.) Gaertn. species [J]. , 2019, 31(8): 1321-1330.
[5]	CAO Yan, XIA Qile, CHEN Jianbing, SHAN Zhichu. Production of bacterial cellulose by Gluconacetobacter xylinus using rice milk [J]. , 2019, 31(11): 1918-1925.