Role of Ovalbumin/β-Cyclodextrin in Improving Structural and Gelling Properties of Culter alburnus Myofibrillar Proteins during Frozen Storage

Meiwen Lv,Rana Muhammad Aadil,Muhammad Hamzah Saleem,Xiukang Wang,Basit Latief Jan,José M Lorenzo,Asad Nawaz,Mario J Simirgiotis,Zhongli Zhang,Shakeel Ahmed,Noman Walayat

doi:10.3390/app112411815

Abstract

This study aimed to analyze the cryoprotective effect of a ovalbumin (OVA) and β-cyclodextrin (βCD) mixture (3:1, OVA/βCD) on the structure, rheology and gelling properties of myofibrillar proteins (MPs) during 90 days of frozen storage. A mixture of OVA/βCD at different concentrations (0, 2, 4, and 6%) was added to MPs and stored at −18 °C for 90 days. The addition of OVA/βCD significantly decreased the sulfhydryl contents while it increased the surface hydrophobicity, which was closely connected with tertiary structural changes. Circular dichroism analysis showed that the addition of OVA/βCD enhanced the stability of the secondary structure by inhibiting the decline in the α-helix. Rheological properties analysis indicated that 6% OVA/βCD treatment showed better storage modulus (G’) and loss modulus (G”). In addition, treatment of OVA/βCD showed better gel forming properties than the control group (0%), helping to form a homogeneous and denser gel network. The results proved that 6% OVA/βCD could be act as a promising cryoprotectant, which can improve the structure and gel behavior of Culter alburnus MPs during frozen storage. Moreover, OVA/βCD could be a potential alternative to conventional cryoprotectants at the industrial level to increase the economic and commercial values of seafood products.

Highlights

Culter alburnus, called as topmouth culter, is an important Chinese freshwater fish due to its abundant availability and consumption [1]
The results demonstrate the broad potential of the OVA/βCD mixture as a promising new cryoprotectant to extend the economic value of Culter alburnus, which has not been reported before in the surimi or seafood industries
Myosin is the major component of myofibrillar proteins (MPs)

Summary

Introduction

Called as topmouth culter, is an important Chinese freshwater fish due to its abundant availability and consumption [1]. It has higher nutritional values, low cholesterol and low polyunsaturated fatty acids that make it important for preservation and commercialization. Freezing and frozen storage is one of the widely used method for long term preservation of fish with minimum deteriorative changes in the quality. During frozen storage, fish proteins undergo various changes that can affect the quality of fish, such as protein and lipid oxidation, resulting in protein denaturation and aggregation. The uncontrolled formation of ice crystals causes protein denaturation and results in more water-soluble proteins [3,4]

Objectives

Methods

Results