The gelling properties of fish gelatin as improved by ultrasound-assisted phosphorylation

Yong Wang; Qinan Cui; Xiuqin Wang; Caiyun Wu; Xianbing Xu; Xiuping Dong; Jinfeng Pan

doi:10.1016/j.foodchem.2024.139214

The gelling properties of fish gelatin as improved by ultrasound-assisted phosphorylation

Food Chem. 2024 Aug 15:449:139214. doi: 10.1016/j.foodchem.2024.139214. Epub 2024 Apr 2.

Authors

Yong Wang¹, Qinan Cui¹, Xiuqin Wang¹, Caiyun Wu¹, Xianbing Xu¹, Xiuping Dong¹, Jinfeng Pan²

Affiliations

¹ National Engineering Research Center for Seafood, State Key Laboratory of Marine Food Processing and Safety Control, Collaborative Innovation Center of Provincial and Ministerial Co-construction for Seafood Deep Processing, Liaoning Province Collaborative Innovation Center for Marine Food Deep Processing, Dalian Technology Innovation Center for Chinese Pre-made Food, College of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.
² National Engineering Research Center for Seafood, State Key Laboratory of Marine Food Processing and Safety Control, Collaborative Innovation Center of Provincial and Ministerial Co-construction for Seafood Deep Processing, Liaoning Province Collaborative Innovation Center for Marine Food Deep Processing, Dalian Technology Innovation Center for Chinese Pre-made Food, College of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China. Electronic address: panjf@dlpu.edu.cn.

PMID: 38581790
DOI: 10.1016/j.foodchem.2024.139214

Abstract

This study investigated the effects of ultrasound-assisted phosphorylation on gelling properties of fish gelatin (FG). Ultrasound-assisted phosphorylation (UP) for 60, 90, and 120 min resulted in >6.54% increase of phosphorylation degree and decreased zeta potential of FG. Atomic force microscopy revealed that UP-FGs showed larger aggregates than P-FGs (normal phosphorylation FGs). Low frequent-NMR and microstructure analysis revealed that phosphorylation enhanced water-binding capability of FG and improved the gel networks. However, UP60 had the highest gel strength (340 g), gelling (17.96 °C) and melting (26.54 °C) temperature while UP90 and UP120 showed slightly lower of them. FTIR analysis indicated thatβ-sheet and triple helix content increased but random coil content decreased in phosphorylated FGs. Mass spectrometry demonstrated phosphate groups mainly bound to serine, threonine and tyrosine residues of FG and UP-FG exhibited more phosphorylation sites. The study showed that mild phosphorylation (UP60) could be applied to improve FG gel properties.

Keywords: Fish gelatin; Gelling properties; Phosphorylation; Ultrasound.

MeSH terms

Animals
Fish Products / analysis
Fish Proteins* / chemistry
Fishes*
Gelatin* / chemistry
Gels* / chemistry
Phosphorylation
Rheology

Substances

Gelatin
Gels
Fish Proteins