Abstract

AbstractAntifreeze proteins (AFPs) modify the ice shape and inhibit further growth leading to thermal hysteresis (TH). Numerous studies have been performed with the addtition of AFPs to preserve frozen products but the influence of sucrose on the effects of AFPs has not been investigated as of yet. Therefore, the TH activities of type I antifreeze protein (AFP I) and antifreeze glycoprotein (AFGP) were measured as a function of concentration, type of AFPs, and also sucrose concentration. The results showed that the TH values rose with increase in concentration of AFPs and sucrose concentration. The crystals experienced shape modification and grew in the c‐axis direction in the presence of both AFPs. The bursting rate of crystals changed depending on both the concentrations of AFPs and sucrose.

Highlights

  • Ice recrystallization (IR), which occurs especially during frozen storage, is an undesired process due to the potential negative effect on the quality of frozen products

  • Regand and Goff suggested that ice structuring proteins (ISPs), which is another name for ice-binding proteins (IBPs), from cold-acclimated winter wheat grass extract can be used to inhibit ice recrystallization [5]

  • The average thermal hysteresis (TH) activities of both antifreeze proteins (AFPs) I and antifreeze glycoprotein (AFGP) rise with higher concentration of proteins

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Summary

Introduction

Ice recrystallization (IR), which occurs especially during frozen storage, is an undesired process due to the potential negative effect on the quality of frozen products. As proposed by Griffith and Ewart, ice-binding proteins (IBPs) have the unique ability to inhibit ice growth and in consequence inhibit recrystallization [4]. Regand and Goff suggested that ice structuring proteins (ISPs), which is another name for IBPs, from cold-acclimated winter wheat grass extract can be used to inhibit ice recrystallization [5]. Gaukel et al revealed that the presence of IBPs in sucrose solutions resulted in a marked decrease in recrystallization [6]. This effect is based on their ice-binding affinity. The freezing point is depressed due to an increase in surface curvature due to the Gibbs-Thomson effect

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