Isolation and characterisation of sericin antifreeze peptides and molecular dynamics modelling of their ice-binding interaction

Jinhong Wu; Yuzhi Rong; Zhengwu Wang; Yanfu Zhou; Shaoyun Wang; Bo Zhao

doi:10.1016/j.foodchem.2014.11.100

Isolation and characterisation of sericin antifreeze peptides and molecular dynamics modelling of their ice-binding interaction

Food Chem. 2015 May 1:174:621-9. doi: 10.1016/j.foodchem.2014.11.100. Epub 2014 Nov 23.

Authors

Jinhong Wu¹, Yuzhi Rong¹, Zhengwu Wang¹, Yanfu Zhou², Shaoyun Wang³, Bo Zhao⁴

Affiliations

¹ Department of Food Science and Engineering, Bor S. Luh Food Safety Research Center, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240, China.
² Department of Food Science, College of Biological Science and Technology, Fuzhou University, Fuzhou 350002, China.
³ Department of Food Science, College of Biological Science and Technology, Fuzhou University, Fuzhou 350002, China. Electronic address: shywang@fzu.edu.cn.
⁴ College of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210097, China.

PMID: 25529728
DOI: 10.1016/j.foodchem.2014.11.100

Abstract

This study aimed to isolate and characterise a novel sericin antifreeze peptide and investigate its ice-binding molecular mechanism. The thermal hysteresis activity of ice-binding sericin peptides (I-SP) was measured and their activity reached as high as 0.94 °C. A P4 fraction, with high hypothermia protective activity and inhibition activity of ice recrystallisation, was obtained from I-SP, and a purified sericin peptide, named SM-AFP, with the sequence of TTSPTNVSTT and a molecular weight of 1009.50 Da was then isolated from the P4 fraction. Treatment of Lactobacillus delbrueckii Subsp. bulgaricus LB340 LYO with 100 μg/ml synthetic SM-AFP led to 1.4-fold increased survival (p < 0.05). Finally, an SM-AFP/ice binding model was constructed and results of molecular dynamics simulation suggested that the binding of SM-AFP with ice and prevention of ice crystal growth could be attributed to hydrogen bond formation, hydrophobic interaction and non-bond interactions. Sericin peptides could be developed into beneficial cryoprotectants and used in frozen food processing.

Keywords: Antifreeze activity; Ice-binding; Isolation; Molecular dynamic modelling; Sericin peptides.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Antifreeze Proteins / chemistry*
Hydrogen Bonding
Ice / analysis*
Models, Molecular
Molecular Dynamics Simulation*
Sericins / chemistry*

Substances

Antifreeze Proteins
Ice
Sericins