Optimizing the formation of myosin/high-density lipoprotein composite gels: PH-dependent effects on heat-induced aggregation

Yuemei Zhang; Hangbin Lyu; Ying Wang; Genpeng Bai; Jinpeng Wang; Wendi Teng; Wei Wang; Jinxuan Cao

doi:10.1016/j.ijbiomac.2024.131786

Optimizing the formation of myosin/high-density lipoprotein composite gels: PH-dependent effects on heat-induced aggregation

Int J Biol Macromol. 2024 Apr 23;268(Pt 2):131786. doi: 10.1016/j.ijbiomac.2024.131786. Online ahead of print.

Authors

Yuemei Zhang¹, Hangbin Lyu², Ying Wang³, Genpeng Bai¹, Jinpeng Wang¹, Wendi Teng¹, Wei Wang⁴, Jinxuan Cao¹

Affiliations

¹ Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, 100048 Beijing, China; Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, 100048 Beijing, China.
² Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, College of Food Science and Pharmaceutical Sciences, Ningbo University, 315211 Ningbo, China.
³ Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Ministry of Education, 100048 Beijing, China; Beijing Engineering and Technology Research Center of Food Additives, School of Food and Health, Beijing Technology and Business University, 100048 Beijing, China. Electronic address: wangying@btbu.edu.cn.
⁴ Key Laboratory of Meat Processing of Sichuan, College of Food and Biological Engineering, Chengdu University, Chengdu 610106, China.

PMID: 38657927
DOI: 10.1016/j.ijbiomac.2024.131786

Abstract

This study investigated impact of high-density lipoprotein (HDL) on thermal aggregation and gelling behavior of myosin in relation to varied pHs. Results revealed that HDL modified myosin structure before and after heating, with distinct effects observed at varied pH. Under pH 5.0, both myosin and HDL-MS exhibited larger aggregates and altered microstructure; at pH 7.0 and 9.0, HDL inhibited myosin aggregation, resulting in enhanced solubility, reduced turbidity and particle size. Comparative analysis of surface hydrophobicity, free sulfhydryl groups and secondary structure highlighted distinct thermal aggregation behavior between MS and HDL-MS, with the latter showing inhibitory effects under neutral or alkaline conditions. Gelation behavior was enhanced at pH 7.0 with maximum strength, hardness, water-holding capacity and rheological properties. Under acidic pH, excessive protein aggregation resulted in increased whiteness and rough microstructure with granular aggregates. Under alkaline pH, gel network structure was weaker, possibly due to higher thermal stability of protein molecules. Scanning electron microscopy revealed expanded HDL protein particles at pH 7.0, accounting for decreased gel strength and altered rheological properties compared with myosin gel. Overall, the results indicated a positive role of HDL at varied pH in regulating thermal aggregation of myosin and further impacting heat-induced gel characteristics.

Keywords: Gelling properties; High-density lipoprotein; Myosin; Thermal aggregation; pH controlling.