Water-soluble myofibrillar protein-pectin complex for enhanced physical stability near the isoelectric point: Fabrication, rheology and thermal property

Xing Chen; Qingyang Qiu; Kaiwen Chen; Di Li; Li Liang

doi:10.1016/j.ijbiomac.2019.10.003

Water-soluble myofibrillar protein-pectin complex for enhanced physical stability near the isoelectric point: Fabrication, rheology and thermal property

Int J Biol Macromol. 2020 Jan 1:142:615-623. doi: 10.1016/j.ijbiomac.2019.10.003. Epub 2019 Oct 14.

Authors

Xing Chen¹, Qingyang Qiu², Kaiwen Chen², Di Li², Li Liang³

Affiliations

¹ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address: xingchen@jiangnan.edu.cn.
² State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
³ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address: liliang@jiangnan.edu.cn.

PMID: 31622714
DOI: 10.1016/j.ijbiomac.2019.10.003

Abstract

This study tested the potential of forming soluble complex with pectin (PEC) on enhancing physical stability of water-soluble myofibrillar protein (WSMP) near the isoelectric point (pI, pH 5.00-5.50). After incorporation of PEC at the mixing ratio of 10:1 and 5:1, WSMP suspension maintained transparent state at 0.05 wt% while a homogeneous monophase at 1.00 wt% around pI, indicating the formation of soluble WSMP-PEC complex. When mixing the two biopolymers, charge neutralization was observed, revealing the electrostatic attraction between positively charged patches of WSMP and negatively charged carboxyl sites of PEC. Steady shear results showed a reduced viscosity of WSMP-PEC complex when dropping the pH to 5.00, this may be related to the declined biopolymer net charge and water trapping. Oscillatory data suggest the formation of highly-interconnected network in soluble WSMP-PEC complex, thus decreasing pH or biopolymer ratio can enhance their interactions and thereby lead to stronger and more stable microstructure. Thermal denaturation temperature of WSMP was significantly enhanced through the formation of WSMP-PEC soluble complexes. Overall, complexation with PEC improved the colloidal and thermal stability of WSMP around the pI, which evidenced the potential of applying tailor designed protein-polysaccharide complex in formulating muscle protein-based beverages.

Keywords: Pectin; Soluble complex; Water-soluble myofibrillar protein.

MeSH terms

Animals
Chickens
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Isoelectric Point
Myofibrils / chemistry*
Pectins / chemistry*
Pectoralis Muscles / chemistry*
Phase Transition
Protein Binding
Protein Conformation
Proteins / chemistry*
Rheology
Solubility
Static Electricity
Temperature
Viscosity
Water

Substances

Proteins
Water
Pectins