Ice-binding proteins: a remarkable ice crystal regulator for frozen foods

Xu, Can; Shi, Xiaodan; Cai, Xiaoyan; Yang, Fujia; Li, Ling; Wu, Jinhong; Wang, Shaoyun

doi:10.1080/10408398.2020.1798354

Cited by 44 publications

(26 citation statements)

References 94 publications

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“…The frost-related damage of microorganisms during storage under freezing conditions is mainly caused by the recrystallization and thawing process 2 , 27 . Therefore, compared with THA, the IRI ability of AFPs is more important for frozen products during storage.…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, compared with THA, the IRI ability of AFPs is more important for frozen products during storage. The preferential adsorption of AFPs on the growth interface of ice to control the ice growth is widely accepted as conferring them their IRI ability and functional role in protecting organisms from freezing damage 14 , 27 – 29 . The IRI of rsfAFP was conducted via a polarized light microscope with a cold stage, and the results are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…), AFPs, with the advantages of less toxicity and non-cell membrane penetration, are becoming the most promising cryoprotectants for the cryopreservation of cells 37 . Although AFPs can more effectively regulate ice crystals than current cryoprotectants at low concentrations, a deeper understanding of their mechanisms of cryopreservation of cells is required 27 .…”

Section: Discussionmentioning

confidence: 99%

“…The cryopreserve effect of AFPs on organisms comes from the non-colligative reduction of AFPs, which inhibits ice crystal recrystallization. Numerous studies have shown that AFPs are specifically adsorbed at the growth interface of ice crystals to increase the growth curvature of ice and increase the vapor pressure of the ice-water interface layer, thereby lowering its freezing point 27 , 32 , 38 . The regulation effect of insect AFPs on ice crystals conforms to the “Janus” effect, which includes non-ice-binding faces (NIBF) and ice-binding faces (IBF) 39 .…”

Section: Discussionmentioning

confidence: 99%

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Snow flea antifreeze peptide for cryopreservation of lactic acid bacteria

et al. 2022

npj Sci Food

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Cryogenic machining is one of the most commonly used techniques for processing and preserving in food industry, and traditional antifreeze agents cannot regulate the mechanical stress damage caused by ice crystals formed during recrystallization or thawing. In this study, we successfully developed an express system of a novel recombinant snow flea antifreeze peptide (rsfAFP), which has significant ice recrystallization inhibition ability, thermal hysteresis activity and alters ice nucleation, thus regulating extracellular ice crystal morphology and recrystallization. We showed that rsfAFP improved the survival rate, acid-producing ability, freezing stability, and cellular metabolism activity of Streptococcus thermophilus. We further showed that rsfAFP interacts with the membrane and ice crystals to cover the outer layer of cells, forming a dense protective layer that maintains the physiological functions of S. thermophilus under freezing stress. These findings provide the scientific basis for using rsfAFP as an effective antifreeze agent for lactic acid bacteria cryopreservation or other frozen food.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Snow flea antifreeze peptide for cryopreservation of lactic acid bacteria

et al. 2022

npj Sci Food

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“…The antifreeze activity determination refers to reported research with minor modifications [ 14 , 25 ]. L. rhamnosus activated overnight at 37 °C in MRS were cultured with an incubation dosage of 2% ( v / v ).…”

Section: Methodsmentioning

confidence: 99%

Antifreeze Peptides Preparation from Tilapia Skin and Evaluation of Its Cryoprotective Effect on Lacticaseibacillus rhamnosus

Zeng

Liu

et al. 2022

Foods

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Antifreeze peptides can protect cell membranes and maintain the cell viability of probiotics under cold stress. Given this, antifreeze peptides were prepared from tilapia processing byproducts of tilapia skin by enzymolysis using the response surface methodology (RSM) method. The cryoprotective effects on Lacticaseibacillus rhamnosus ATCC7469 were investigated. Trypsin was selected as the protease for tilapia skin hydrolysis. The optimal hydrolysis conditions consisted of the amount of enzyme (2200 U/g), solid–liquid ratio (1:10, w/v), reaction temperature (49 °C), and reaction time (6.8 h), and the relative survival rate of L. rhamnosus reached 98.32%. Molecular weight (Mw) distribution and peptide sequences of the antifreeze peptides prepared from tilapia skin (APT) under the optimal conditions were analyzed. APT significantly reduced the leakage of extracellular proteins and protected β-galactosidase and lactate dehydrogenase activities of L. rhamnosus. Compared with the saline group, scanning electron microscopy (SEM) observation showed that cells had a more normal, smooth, and entire surface under the protection of APT. These findings indicate that APT can be a new cryoprotectant in preserving probiotics.

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Cryoprotective effect of glycopeptide complex from abalone viscera on frozen surimi and its underlying mechanism

Chen,

Yu,

et al. 2024

Food Frontiers

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Freezing technology is important for the long‐term preservation of aquatic products such as surimi. However, mechanical damage caused by ice crystals would lead to quality deterioration. Abalone viscera glycopeptide (AVGP) complex was prepared by hydrolysis technology, which exhibited ice recrystallization ability and antioxidant activity. Moreover, effects of AVGP on Ca2+‐ATPase activity, total sulfhydryl content, secondary structure of myofibrillar protein (MP), rheological properties, and gel properties of surimi frozen were investigated. Results showed that surimi treated with AVGP could improve the gel strength and rheological properties of surimi, reduce the gel ice crystal holes, and improve the degradation of gel matrix caused by freeze–thaw. AVGP can significantly inhibit the decrease of Ca2+‐ATPase activity and total sulfhydryl group content. When the addition of AVGP exceeded 4% (w/w), its freezing protection effect on MP was better than that of commercial antifreeze agents. Moreover, the α‐helix and β‐fold contents in the 4% AVGP group were significantly higher than those in the control group, indicating that the addition of an appropriate amount of AVGP can protect the secondary structure of MP. Therefore, AVGP could serve as a new food ingredient with antifreeze and antioxidant functions for frozen surimi.

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Ice-binding proteins: a remarkable ice crystal regulator for frozen foods

Cited by 44 publications

References 94 publications

Snow flea antifreeze peptide for cryopreservation of lactic acid bacteria

Snow flea antifreeze peptide for cryopreservation of lactic acid bacteria

Antifreeze Peptides Preparation from Tilapia Skin and Evaluation of Its Cryoprotective Effect on Lacticaseibacillus rhamnosus

Cryoprotective effect of glycopeptide complex from abalone viscera on frozen surimi and its underlying mechanism

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