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To optimize the preparation method of highly active cod gelatin antifreeze peptides (DcAFPs) and clarify its cryoprotective effects on surimi, this study added cod gelatin peptides to surimi. The myofibrillar protein content in the surimi after freezing was used as an evaluation index, and the process was optimized through single-factor and orthogonal experiments. By determining the molecular weight distribution and amino acid composition of DcAFPs, their basic properties were analyzed. Additionally, the protective effects of DcAFPs on surimi subjected to repeated freeze-thaw cycles were assessed by measuring myofibrillar protein content and utilizing intrinsic fluorescence spectroscopy and SDS-PAGE gel electrophoresis techniques. The results showed that the optimal preparation process for DcAFPs involved using compound protease, with a substrate concentration of 3.5% (w/v), an enzyme-to-substrate ratio of 5% (w/w), a hydrolysis pH of 8, a hydrolysis temperature of 55 ℃, and a hydrolysis time of 2 hours. The molecular weight of DcAFPs was primarily concentrated between 185 and 3081 Da, with glycine (Gly), alanine (Ala), and glutamic acid (Glu) being the most abundant amino acids. DcAFPs effectively prevented the reduction of myofibrillar protein content during freeze-thaw cycles, inhibited changes in the structure and composition of myofibrillar proteins, and delayed protein denaturation. In conclusion, DcAFPs exhibited significant cryoprotective effects on surimi that subjected to repeated freeze-thaw cycles and outperformed commercial antifreeze agents.

Summary: Enzymatic supramolecular assembly was applied to increase the thermal hysteresis activity (THA) of tilapia skin collagen peptides and their applicability as cryoprotectants. The THA value of the glutamine‐assembled product increased by 61.5% and its ice crystal content dropped by 33.93% compared to the collagen peptides. Following initial separation and purification, the THA of Gln‐AFPs was further elevated by 28.6%. After five freeze–thaw cycles, tilapia surimi treated with 8% Gln‐AFPs had high levels of salt‐soluble protein, total sulfhydryl content, Ca2+‐ATPase activity, and water‐holding capacity. Additionally, the cryoprotective effect of Gln‐AFPs on the surimi was found to be superior to that of commercial antifreeze. The majority of the Gln‐AFPs turns folded, according to FTIR analysis, and ‐helices were produced. After supramolecular assembly, the Gln‐AFPs structure also smoothed out. As a result, the enzymatic supramolecular assembly drastically increased the antifreeze activity of the tilapia skin‐collagen peptides, which could eventually be developed into a novel antifreeze additive in the food industry. [ABSTRACT FROM AUTHOR]

A new antifreeze agent was prepared from Egg White Protein (EWP) and β-Cyclodextrin (β-CD). Through single factor experiments and response surface test, the preparation conditions of EWP-β-CD complex with the best antifreeze activity were obtained. Then EWP-β-CD complex with different concentrations (2%, 4% and 6%) was applied to the four freeze-thaw cycle system of shrimp to study the antifreeze protection of EWP-β-CD complex on shrimp. The results showed that the optimum conditions for the preparation of EWP-β-CD composite system were pH7.0, the composite ratio of β-CD and EWP 1:10, the heat treatment temperature 75 ℃. The antifreeze activity of EWP-β-CD composite system was 84.09%±1.06% under the optimal conditions. The EWP-β-CD complex under this condition was applied to the freeze-thaw cycle of shrimp. After adding EWP-β-CD complex, the water retention, hardness and chewability of shrimps were significantly improved, and the chromaticity of shrimps was not significantly affected. When the addition of EWP-β-CD complex was 4% and 6%, the effect of EWP-β-CD complex on protein degradation and fat oxidation of shrimp was significantly better than that of commercial antifreeze. The preparation conditions of EWP-β-CD complex are optimized by response surface method, and it was preliminarily showed that it had a certain protective effect on the quality of shrimp. This result would provide a theoretical basis for the subsequent development of low sweetness and low calorie antifreeze.

Ice formation on a solid surface is a major challenge in industrial applications, it causes higher energy consumption and performance deterioration and may lead to catastrophic results. The preparation of anti‐icing surfaces to prohibit ice accumulation on a surface is crucial to reduce operational costs and to extend the surface's lifetime. The utilization of cryoprotectants to obtain anti‐icing surfaces is an effective method and is applicable in multiple fields. Antifreeze proteins (AFPs) are natural cryoprotectants to obtain anti‐icing surfaces, which have the ability to decrease the freezing point and to prevent ice‐crystal growth via thermal hysteresis (TH) and ice recrystallization inhibition (IRI). This study reports the molecular cloning, expression, and production of AFP protein from Escherichia coli (E. Coli). This wok also demonstrates the activity of coated AFP on aluminum surfaces. The expressed AFP is immobilized on aluminum surfaces treated by oxygen plasma. The coated AFP exhibits promising antifreeze activity with a high anti‐icing ability on aluminum surfaces in the size of evaporator fins (40 × 40 cm). The outcome of this study provides new insights into the biotechnological implementation of AFPs to various industrial applications for energy‐saving and higher performance. [ABSTRACT FROM AUTHOR]

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Abstract Ice formation on a solid surface is a major challenge in industrial applications, it causes higher energy consumption and performance deterioration and may lead to catastrophic results. The preparation of anti‐icing surfaces to prohibit ice accumulation on a surface is crucial to reduce operational costs and to extend the surface's lifetime. The utilization of cryoprotectants to obtain anti‐icing surfaces is an effective method and is applicable in multiple fields. Antifreeze proteins (AFPs) are natural cryoprotectants to obtain anti‐icing surfaces, which have the ability to decrease the freezing point and to prevent ice‐crystal growth via thermal hysteresis (TH) and ice recrystallization inhibition (IRI). This study reports the molecular cloning, expression, and production of AFP protein from Escherichia coli (E. Coli). This wok also demonstrates the activity of coated AFP on aluminum surfaces. The expressed AFP is immobilized on aluminum surfaces treated by oxygen plasma. The coated AFP exhibits promising antifreeze activity with a high anti‐icing ability on aluminum surfaces in the size of evaporator fins (40 × 40 cm). The outcome of this study provides new insights into the biotechnological implementation of AFPs to various industrial applications for energy‐saving and higher performance.

A cryoprotectant known as ice-binding protein (IBP) is thought to facilitate the cold survival of plants, insects, and fungi. Here, we prepared a genetically modified Caenorhabditis elegans strain to synthesize fish-derived IBPs in its body wall muscles and examined whether the antifreeze activity modification of this IBP by point mutation affects the cold tolerance of this worm. We chose a 65-residue IBP identified from notched-fin eelpout, for which the replacement of the 20th alanine residue (A20) modifies its antifreeze activity. These mutant proteins are denoted A20L, A20G, A20T, A20V, and A20I along with the wild-type (WT) protein. We evaluated the survival rate (%) of the transgenic C. elegans that synthesized each IBP mutant following 24 h of preservation at −5, +2, and +5 °C. Significantly, a dramatic improvement in the survival rate was detected for the worms synthesizing the activity-enhanced mutants (A20T and A20I), especially at +2 °C. In contrast, the rate was not improved by the expression of the defective mutants (A20L, A20G, WT and A20V). The survival rate (%) probably correlates with the antifreeze activity of the IBP. These data suggest that IBP protects the cell membrane by employing its ice-binding mechanism, which ultimately improves the cold tolerance of an IBP-containing animal. • Ice-binding protein (IBP) improves the cold tolerance of transgenic C. elegans. • IBP activity improvement affects the survival rate of C. elegans. • Cell protection and ice binding by IBPs may originate from the same mechanism. [ABSTRACT FROM AUTHOR]

In this study, the effects of thermal hysteresis activity, ice recrystallization inhibition, amino acid composition and surface hydrophobicity of different ultrasonic pretreatments on gluten antifreeze polypeptide was studied. The results of the thermal hysteresis activity showed that the collaborative (flat-panel combined probe) ultrasonic working mode was superior to the single-frequence ultrasound mode. In the optimal working mode (15 min, 100 W/L), the results of polarized light microscope and gel chromatography column showed that ultrasonic pretreatment could effectively inhibit the growth of ice crystals, reduced the size of ice crystals, and to a certain extent, transfer the molecular weight distribution of peptides to small molecular peptides. The molecular weight was mainly concentrated at about 200–1000 u. The contents of Valine, Methionine, Leucine, Proline and Glutamic acid residues in the gluten antifreeze polypeptide pretreated by ultrasonic wave were relatively high and more hydrophobic groups were exposed. The secondary structure results showed that the molecular conformation of the polypeptide was mainly α-helix and β-sheet conformations. This paper systematically revealed the intrinsic correlation mechanism between the changes of key domains of substrate proteins and the antifreeze activity of enzymatic hydrolysis products assisted by ultrasoud, providing a theoretical basis for the preparation of antifreeze polypeptide. • Ultrasonic pretreatment improved the thermal hysteresis activity of gluten antifreeze peptides. • Ultrasonic pretreatment exposed more hydrophobic groups of gluten antifreeze peptides. • The molecular conformation of gluten antifreeze polypeptide was mainly α-helix and β-sheet conformations. [ABSTRACT FROM AUTHOR]

The structure of frozen dough was damaged due to the recrystallization of ice crystals during freeze-thawing. Therefore, the effect of bovine hide gelatin antifreeze peptides (BgAFPs) on the quality of frozen dough treated with freeze-thaw cycles and its steamed bread was investigated. The results showed that BgAFPs exhibited a high thermal hysteresis activity at 1.64 °C and possessed the significant ability to inhibit ice crystals growth due to its -Gly-X-Y- (where X was mostly proline or hydroxyproline, Y was any amino acid) repeating sequences. The decrease in gassing rate of frozen dough without BgAFPs (41.31%) was significantly greater than those of frozen dough with BgAFPs (36.32%, 27.74% and 24.30%), revealing that the BgAFPs had cryoprotective effect on yeast cells. Additionally, BgAFPs maintained a continuous apparent morphology of the frozen dough by inhibiting water migration. Specifically, the freezable water content in the frozen dough with 0% and 1.0% BgAFPs increased from 63.35% and 59.41% to 73.74% and 64.36%, respectively. Furthermore, BgAFPs increased the specific volume and springiness, decreased the hardness of the steamed bread. These results suggested that BgAFPs effectively attenuated the freeze-thaw induced damage to frozen dough and improved the quality of steamed bread. [Display omitted] • BgAFPs exhibited a maximum THA of 1.64 °C and inhibited ice crystal growth. • BgAFPs provided cryoprotective effect on yeast cells. • BgAFPs decreased freezable water content and water mobility of frozen dough. • BgAFPs maintained the dense and continuous microstructure of the frozen dough. • BgAFPs attenuated the textural deterioration of frozen dough steamed bread. [ABSTRACT FROM AUTHOR]

Antifreeze proteins (AFPs) protecting the cells against freezing are produced in response to extremely low temperatures in diverse psychrophilic organisms, and they are encoded by multiple gene families. The AFP of Antarctic marine diatom Chaetoceros neogracile is reported in our previous research, but like other microalgae, was considered to probably have additional genes coding AFPs. In this paper, we reported the cloning and characterization of additional AFP gene from C. neogracile (Cn-isoAFP). Cn-isoAFP protein is 74.6% identical to the previously reported Cn-AFP. The promoter sequence of Cn-isoAFP contains environmental stress responsive elements for cold, thermal, and high light conditions. Cn-isoAFP transcription levels increased dramatically when cells were exposed to freezing (--20 °C), thermal (10 °C), or high light (600 μmol photon m-2 s-1) stresses. The thermal hysteresis (TH) activity of recombinant Cn-isoAFP was 0.8 °C at a protein concentration of 5 mg/mL. Results from homology modeling and TH activity analysis of site-directed mutant proteins elucidated AFP mechanism to be a result of flatness of B-face maintained via hydrophobic interactions. [ABSTRACT FROM AUTHOR]

The cryoprotective effect of collagen hydrolysates from squid skin (CH-SS) on shrimp muscle was investigated during the freeze-thaw cycles, and the antifreeze peptides (AFPs) in CH-SS were separated and identified. The results showed that CH-SS generated by acid protease had the highest antifreeze activity. It was further found that CH-SS showed an inhibitory effect on the denaturation and structural changes of myofibrillar protein during the freeze-thaw cycles, and partially retained the ability to bind water. SEM analysis indicated that CH-SS could effectively reduce the mechanical injury caused by ice crystals to shrimp muscle. The fraction with the highest antifreeze activity from CH-SS was obtained by Sephadex G-25 chromatography, and its main amino acid sequence was identified as DVRGAEGSAGL by the UPLC-MS analysis. This study provides a theoretical basis for the intensive processing of squid skin and the development of new antifreeze agents. • CH-SS generated by acid protease had a high antifreeze activity. • CH-SS had a better cryoprotective effect on shrimp muscle than that of TSPP. • Antifreeze activity of F 2 was significantly higher than that of CH-SS. • Amino acid sequence of F 2 was identified as DVRGAEGSAGL. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

Overwintering plants secrete antifreeze proteins (AFPs) to provide freezing tolerance. These proteins bind to and inhibit the growth of ice crystals that are formed in the apoplast during subzero temperatures. Antifreeze activity has been detected in more than 60 plants and AFPs have been purified from 15 of these, including gymnosperms, dicots and monocots. Biochemical characterization of plant antifreeze activity, as determined by the high ice recrystallization inhibition (IRI) activities and low thermal hysteresis (TH) of AFPs, showed that their main function is inhibition of ice crystal growth rather than the lowering of freezing temperatures. However, recent studies showed that antifreeze activity with higher TH also exists in plants. Calcium and hormones like ethylene and jasmonic acid have been shown to regulate plant antifreeze activity. Recent studies have shown that plant AFPs bind to both prism planes and basal planes of ice crystals by means of two flat ice binding sites. Plant AFPs have been postulated to evolve from the OsLRR-PSR gene nearly 36 million years ago. In this review, we present the current scenario of plant AFP research in order to understand the possible potential of plant AFPs in generation of freezing-tolerant crops. [ABSTRACT FROM AUTHOR]

Freeze-thaw stress has previously been shown to alter soil community structure and function. We sought to further investigate this stress on enriched microbial consortia with the aim of identifying microbes with ice-associating adaptations that facilitate survival. Enrichments were established to obtain culturable psychrotolerant microbes from soil samples from the latitudinal extremes of the Canadian Shield plateau. The resulting consortia were subjected to consecutive freeze-thaw cycles, and survivors were putatively identified by their 16S rRNA gene sequences. Even though the northerly site was exposed to longer, colder winters and large spring-time temperature fluctuations, the selective regime similarly affected both enriched consortia. Quantitative PCR and metagenomic sequencing were used to determine the frequency of a subset of the resistant microbes in the original enrichments. The metagenomes showed 22 initial genera, only 6 survived and these were not dominant prior to selection. When survivors were assayed for ice recrystallization inhibition and ice nucleation activities, over 60% had at least one of these properties. These phenotypes were not more prevalent in the northern enrichment, indicating that regarding these adaptations, the enrichment strategy yielded seemingly functionally similar consortia from each site. [ABSTRACT FROM AUTHOR]

Abstract: Antifreeze proteins (AFPs), characterized by their ability to separate the melting and growth temperatures of ice and to inhibit ice recrystallization, play an important role in cold adaptation of several polar and cold-tolerant organisms. Recently, a multigene family of AFP genes was found in the diatom Fragilariopsis cylindrus, a dominant species within polar sea ice assemblages. This study presents the AFP from F. cylindrus set in a molecular and crystallographic frame. Differential protein expression after exposure of the diatoms to environmentally relevant conditions underlined the importance of certain AFP isoforms in response to cold. Analyses of the recombinant AFP showed freezing point depression comparable to the activity of other moderate AFPs and further enhanced by salt (up to 0.9°C in low salinity buffer, 2.5°C at high salinity). However, unlike other moderate AFPs, its fastest growth direction is perpendicular to the c-axis. The protein also caused strong inhibition of recrystallization at concentrations of 1.2 and 0.12μM at low and high salinity, respectively. Observations of crystal habit modifications and pitting activity suggested binding of AFPs to multiple faces of the ice crystals. Further analyses showed striations caused by AFPs, interpreted as inclusion in the ice. We suggest that the influence on ice microstructure is the main characteristic of these AFPs in sea ice. [Copyright &y& Elsevier]

Abstract: Thermal hysteresis (TH) readings depend on the cooling rate, annealing time and the concentration of the biological antifreeze (AF) (i.e., antifreeze protein or antifreeze glycoprotein). Such time- and concentration-dependent TH readings are not true (or absolute) values. The true TH should be independent of time and AF concentration, and it should be a unique value for a given AF. Only the true TH can be used to assess the activity of an AF. A mathematical model is proposed to explain the time- and concentration-dependent behavior of AFs. The model assumes a reversible Langmuir adsorption mechanism for the AF molecules and the Kelvin effect to be applicable. A TH equation that correlates the TH reading with the cooling rate, annealing time and AF concentration was derived. The time-dependent behavior was attributed to the slow adsorption process of the AF. The theoretical calculations were compared with previously published data on the effects of the cooling rate, annealing time and AF concentration on TH readings. The calculated results agree qualitatively with the literature data. The experimental methodology required for obtaining the true TH of an AF is suggested. [Copyright &y& Elsevier]

Abstract: Antifreeze proteins are a structurally diverse group of proteins characterized by their unique ability to cause a separation of the melting- and growth-temperatures of ice. These proteins have evolved independently in different kinds of cold-adapted ectothermic animals, including insects and fish, where they protect against lethal freezing of the body fluids. There is a great variability in the capacity of different kinds of antifreeze proteins to evoke the antifreeze effect, but the basis of these differences is not well understood. This study reports on salt-induced enhancement of the antifreeze activity of an antifreeze protein from the longhorn beetle Rhagium inquisitor (L.). The results imply that antifreeze activity is predetermined by a steady-state distribution of the antifreeze protein between the solution and the ice surface region. The observed salt-induced enhancement of the antifreeze activity compares qualitatively and quantitatively with salt-induced lowering of protein solubility. Thus, salts apparently enhance antifreeze activity by evoking a solubility-induced shift in the distribution pattern of the antifreeze proteins in favour of the ice. These results indicate that the solubility of antifreeze proteins in the solution surrounding the ice crystal is a fundamental physiochemical property in relation to their antifreeze potency. [Copyright &y& Elsevier]

The insect spruce budworm ( Choristoneura fumiferana) produces antifreeze protein (AFP) to assist in the protection of the over-wintering larval stage and contains multiple isoforms. Structures for two isoforms, known as CfAFP-501 and CfAFP-337, show that both possess similar left-handed β-helical structure, although thermal hysteresis activity of the longer isoform CfAFP-501 is three times that of CfAFP-337. The markedly enhanced activity of CfAFP-501 is not proportional to, and cannot be simply accounted for, by the increased ice-binding site resulting from the two extra coils in CfAFP-501. In order to investigate the molecular basis for the activity difference and gain better understanding of AFPs in general, we have employed several different computational methods to systematically study the structural properties and ice interactions of the AFPs and their deletion models. In the context of intact AFPs, a majority of the coils in CfAFP-501 has better ice interaction and causes stronger ice lattice disruption than CfAFP-337, strongly suggesting a cooperative or synergistic effect among β-helical coils. The synergistic effect would play a critical role and make significant contributions to the antifreeze activity β-helical antifreeze proteins. This is the first time that synergistic effect and its implication for antifreeze activity are reported for β-helical antifreeze proteins. [ABSTRACT FROM AUTHOR]

Abstract: Antifreeze proteins are characterised by their ability to prevent ice from growing upon cooling below the bulk melting point. This displacement of the freezing temperature of ice is limited and at a sufficiently low temperature a rapid ice growth takes place. The separation of the melting and freezing temperature is usually referred to as thermal hysteresis, and the temperature of ice growth is referred to as the hysteresis freezing point. The hysteresis is supposed to be the result of an adsorption of antifreeze proteins to the crystal surface. This causes the ice to grow as convex surface regions between adjacent adsorbed antifreeze proteins, thus lowering the temperature at which the crystal can visibly expand. The model requires that the antifreeze proteins are irreversibly adsorbed onto the ice surface within the hysteresis gap. This presupposition is apparently in conflict with several characteristic features of the phenomenon; the absence of superheating of ice in the presence of antifreeze proteins, the dependence of the hysteresis activity on the concentration of antifreeze proteins and the different capacities of different types of antifreeze proteins to cause thermal hysteresis at equimolar concentrations. In addition, there are structural obstacles that apparently would preclude irreversible adsorption of the antifreeze proteins to the ice surface; the bond strength necessary for irreversible adsorption and the absence of a clearly defined surface to which the antifreeze proteins may adsorb. This article deals with these apparent conflicts between the prevailing theory and the empirical observations. We first review the mechanism of thermal hysteresis with some modifications: we explain the hysteresis as a result of vapour pressure equilibrium between the ice surface and the ambient fluid fraction within the hysteresis gap due to a pressure build-up within the convex growth zones, and the ice growth as the result of an ice surface nucleation event at the hysteresis freezing point. We then go on to summarise the empirical data to show that the dependence of the hysteresis on the concentration of antifreeze proteins arises from an equilibrium exchange of antifreeze proteins between ice and solution at the melting point. This reversible association between antifreeze proteins and the ice is followed by an irreversible adsorption of the antifreeze proteins onto a newly formed crystal plane when the temperature is lowered below the melting point. The formation of the crystal plane is due to a solidification of the interfacial region, and the necessary bond strength is provided by the protein “freezing” to the surface. In essence: the antifreeze proteins are “melted off” the ice at the bulk melting point and “freeze” to the ice as the temperature is reduced to subfreezing temperatures. We explain the different hysteresis activities caused by different types of antifreeze proteins at equimolar concentrations as a consequence of their solubility features during the phase of reversible association between the proteins and the ice, i.e., at the melting point; a low water solubility results in a large fraction of the proteins being associated with the ice at the melting point. This leads to a greater density of irreversibly adsorbed antifreeze proteins at the ice surface when the temperature drops, and thus to a greater hysteresis activity. Reference is also made to observations on insect antifreeze proteins to emphasise the general validity of this approach. [Copyright &y& Elsevier]

Deschampsia antarctica and Colobanthus quitensis are the only vascular plants to have colonized the Maritime Antarctic, which is characterized by its permanently low temperature and frequent summer frosts. To understand how the plants survive freezing temperatures year-round, antifreeze activity was assayed in apoplastic extracts obtained from both non-acclimated and cold-acclimated Antarctic plants. By observing the shape of ice crystals grown in dilution series of the extracts, it was found that D. antarctica had antifreeze activity, but C. quitensis did not. D. antarctica exhibited antifreeze activity in the non-acclimated state and this activity increased after cold acclimation. The antifreeze activity in D. antarctica was labile to proteolysis and high temperature, active over a wide pH range, and associated with molecules greater than 10 kDa in molecular weight. These results show that D. antarctica produces antifreeze proteins that are secreted into the apoplast. When examined by SDS-PAGE, the apoplastic extracts from cold-acclimated D. antarctica exhibited 13 polypeptides. It is concluded that D. antarctica accumulates AFPs as part of its mechanism of freezing tolerance. Moreover, this is the first plant in which antifreeze activity has been observed to be constitutive. [ABSTRACT FROM PUBLISHER]

The paper deals with the study of the ice nucleation activity of the cells, extracellular lipopolysaccharides (ELPSs), lipopolysaccharides (LPSs), and LPS structural components (lipid A, core oligosaccharide, and O-specific polysaccharide) of Pseudomonas fluorescens, P. syringae, P. fragi, and P. pseudoalcaligenes. Aqueous suspensions of intact cells of P. syringae IMV 1951 and IMV 185 began to freeze at –1 and –4°C, respectively. This suggests that these cells possess ice nucleation activity. Aqueous cell suspensions of two other strains, P. fluorescens IMV 1433 and IMV 2125, began to freeze at lower temperatures than did distilled water (–9°C), which suggests that the cells of these strains possess antifreeze activity. The ice nucleation activity of the bacterial strains studied did not show any correlation with their taxonomic status. The ice nucleation activity of ELPSs depended little on their concentration (within a concentration range of 0.2–0.4%). In most cases, the ice nucleation activity of ELPSs, LPSs, and LPS structural components differed from that of the intact cells from which these biopolymers were obtained. This may indicate that the biopolymers under study play a role in ice nucleation but this role is not crucial. The relationship between the structure of LPSs and their effect on ice nucleation is discussed. [ABSTRACT FROM AUTHOR]

Various enantiomeric isomers, metals salts and molecular sizes of poly(γ-glutamic acid), γ-PGA, produced by Bacillus licheniformis CCRC 12826, were prepared and their antifreeze activities were studied by differential scanning calorimetry. The antifreeze activity of γ-PGA increased as its molecular weight decreased but was indifferent to its d/l-glutamate composition. The antifreeze activity was cation dependent decreasing in the order Mg2+>>Ca2+∼Na+>>K+ which follows that of inorganic chlorides in that high ionic charge leads to high antifreeze activity. The mechanism by which the cryoprotective effects of γ-PGA can be explained is still yet to be determined. [ABSTRACT FROM AUTHOR]