Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing-Thawing Cycles

Zhongli Zhang; Zhouyi Xiong; Noman Walayat; Jose M Lorenzo; Jianhua Liu; Asad Nawaz; Hanguo Xiong

doi:10.3390/antiox11010032

Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing-Thawing Cycles

Antioxidants (Basel). 2021 Dec 24;11(1):32. doi: 10.3390/antiox11010032.

Authors

Zhongli Zhang¹, Zhouyi Xiong², Noman Walayat³, Jose M Lorenzo^{4

5}, Jianhua Liu³, Asad Nawaz⁶, Hanguo Xiong¹

Affiliations

¹ College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
² Fisheries Research Institute, Wuhan Academy of Agricultural Sciences, Wuhan 430207, China.
³ College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, China.
⁴ Centro Tecnológico de la Carne de Galicia, Avd. Galicia nº 4, Parque Tecnológico de Galicia, San Cibrao das Viñas, 32900 Ourense, Spain.
⁵ Área de Tecnología de los Alimentos, Facultad de Ciencias de Ourense, Universidad de Vigo, 32004 Ourense, Spain.
⁶ Jiangsu Key Laboratory of Crop Genetics and Physiology, College of Agriculture, Yangzhou University, Yangzhou 225009, China.

Abstract

This study aims to investigate the influence of the mixture (CGO/EWP) of carrageenan oligosaccharide (CGO) and egg white protein (EWP) (CGO/EWP, CGO: EWP = 1:1, m/m) on the functional, structural, and gelling properties of Culter alburnus myofibrillar protein (MP) during repeated freezing-thawing cycles by treating MP samples separately with EWP, CGO, or CGO/EWP based on the wet weight (1%, m/m), using samples without any cryoprotectant as the blank group. After the second repeated freezing-thawing cycle, the sulfhydryl group content was found to be significantly (p < 0.05) higher in the CGO/EWP (30.57 nmol/mg) and CGO (36.14 nmol/mg) groups than in the EWP group (23.80 nmol/mg), indicating that CGO/EWP and CGO can more effectively delay the oxidative deterioration of functional groups. Additionally, the surface hydrophobicity was shown to be significantly lower in the CGO (25.74) and CGO/EWP (27.46) groups than in the EWP (34.66) and blank (39.32) groups. Moreover, the α-helix content was higher in the CGO (35.2%) and CGO/EWP (32.3%) groups than in the EWP (29.2%) and blank (25.0%) groups. These data indicated that CGO and CGO/EWP could more effectively increase the structural stability, thereby inhibiting the exposure of hydrophobic groups and curbing the decline of α-helix content. During the heat-induced gel-forming process, EWP and CGO/EWP could enhance the gel viscoelasticity and strength. After the second freezing-thawing cycle, when compared with the blank group, the CGO/EWP group showed significantly (p < 0.05) higher water-holding capacity (66.30% versus 53.93%) and shorter T₂₂ relaxation time (413.56 versus 474.99 ms). The integrated results indicated that CGO/EWP could more effectively delay the decrease of protein-water molecular interaction forces in the MP gel. This study shed light on the mechanism of CGO/EWP as a cryoprotective mixture in improving the deterioration of MP gelation properties during repeated freezing-thawing cycles.

Keywords: Culter alburnus; carrageenan oligosaccharide; egg white protein; gelation properties; myofibrillar protein.