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Journal articles on the topic 'Ice nucleation protein'

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Published: 4 June 2021

Last updated: 4 February 2022

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1

Bissoyi, Akalabya, Naama Reicher, Michael Chasnitsky, Sivan Arad, Thomas Koop, Yinon Rudich, and Ido Braslavsky. "Ice Nucleation Properties of Ice-binding Proteins from Snow Fleas." Biomolecules 9, no. 10 (September 25, 2019): 532. http://dx.doi.org/10.3390/biom9100532.

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Ice-binding proteins (IBPs) are found in many organisms, such as fish and hexapods, plants, and bacteria that need to cope with low temperatures. Ice nucleation and thermal hysteresis are two attributes of IBPs. While ice nucleation is promoted by large proteins, known as ice nucleating proteins, the smaller IBPs, referred to as antifreeze proteins (AFPs), inhibit the growth of ice crystals by up to several degrees below the melting point, resulting in a thermal hysteresis (TH) gap between melting and ice growth. Recently, we showed that the nucleation capacity of two types of IBPs corresponds to their size, in agreement with classical nucleation theory. Here, we expand this finding to additional IBPs that we isolated from snow fleas (the arthropod Collembola), collected in northern Israel. Chemical analyses using circular dichroism and Fourier-transform infrared spectroscopy data suggest that these IBPs have a similar structure to a previously reported snow flea antifreeze protein. Further experiments reveal that the ice-shell purified proteins have hyperactive antifreeze properties, as determined by nanoliter osmometry, and also exhibit low ice-nucleation activity in accordance with their size.

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2

Mueller, Gunhild M., Paul K. Wolber, and Gareth J. Warren. "Clustering of ice nucleation protein correlates with ice nucleation activity." Cryobiology 27, no. 4 (August 1990): 416–22. http://dx.doi.org/10.1016/0011-2240(90)90018-y.

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3

Lorv, Janet S. H., David R. Rose, and Bernard R. Glick. "Bacterial Ice Crystal Controlling Proteins." Scientifica 2014 (2014): 1–20. http://dx.doi.org/10.1155/2014/976895.

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Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large ice crystals, while ice nucleation proteins induce formation of embryonic ice crystals. Although both protein classes have differing functions, these proteins use the same ice binding mechanisms. Rather than direct binding, it is probable that these protein classes create an ice surface prior to ice crystal surface adsorption. Function is differentiated by molecular size of the protein. This paper reviews the similar and different aspects of bacterial antifreeze and ice nucleation proteins, the role of these proteins in freezing tolerance, prevalence of these proteins in psychrophiles, and current mechanisms of protein-ice interactions.

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4

Hartmann, S., S. Augustin, T. Clauss, J. Voigtländer, D. Niedermeier, H. Wex, and F. Stratmann. "Immersion freezing of ice nucleating active protein complexes." Atmospheric Chemistry and Physics Discussions 12, no. 8 (August 21, 2012): 21321–53. http://dx.doi.org/10.5194/acpd-12-21321-2012.

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Abstract. Biological particles, e.g. bacteria and their Ice Nucleating Active (INA) protein complexes, might play an important role for the ice formation in atmospheric mixed-phase clouds. Therefore, the immersion freezing behavior of INA protein complexes generated from a SnomaxTM solution/suspension was investigated as function of temperature in a range of −5 °C to −38 °C at the Leipzig Aerosol Cloud Interaction Simulator (LACIS). The immersion freezing of droplets containing small numbers of INA protein complexes occurs in a temperature range of −7 °C and −10 °C. The experiments performed in the lower temperature range, where all droplets freeze which contain at least one INA protein complex, are used to determine the average number of INA protein complexes present, assuming that the INA protein complexes are Poisson distributed over the droplet ensemble. Knowing the average number of INA protein complexes, the heterogeneous ice nucleation rate and rate coefficient of a single INA protein complex is determined by using the newly-developed CHESS model (stoCHastic model of idEntical poiSSon distributed ice nuclei). Therefore, we assume the ice nucleation process to be of stochastic nature, and a parameterization of the INA protein complex's nucleation rate. Analyzing the results of immersion freezing experiments from literature (SnomaxTM and Pseudomonas syringae bacteria), to results gained in this study, demonstrates that first, a similar temperature dependence of the heterogeneous ice nucleation rate for a single INA protein complex was found in all experiments, second, the shift of the ice fraction curves to higher temperatures can be explained consistently by a higher average number of INA protein complexes being present in the droplet ensemble, and finally the heterogeneous ice nucleation rate of one single INA protein complex might be also applicable for intact Pseudomonas syringae bacteria cells. The results obtained in this study allow a new perspective on the interpretation of immersion freezing experiments considering INA protein complexes and the derived simple parameterization of the heterogeneous ice nucleation rate can be used in cloud resolving models for studying the effect of bacteria induced ice nucleation.

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5

DU, NING, X. Y. LIU, H. LI, and CHOY LEONG HEW. "THE ROLE OF ANTIFREEZE PROTEIN TYPE I IN ICE NUCLEATION INHIBITION." Biophysical Reviews and Letters 01, no. 03 (July 2006): 271–78. http://dx.doi.org/10.1142/s1793048006000197.

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The effect of Antifreeze Protein Type I (AFP I, one type of fish antifreeze protein) on ice crystallization was examined quantitatively based on a "micro-sized ice nucleation" technique. It is found that Antifreeze Proteins can inhibit the ice nucleation process by adsorbing onto both the surface of ice nuclei and that of foreign dusts. This leads to an increase of the ice nucleation barrier and the desolvation kink kinetics barrier. Based on the latest nucleation model, the increases in the ice nucleation barrier and the kink kinetics barrier were measured. This enables us to quantitatively examine the antifreeze mechanism of AFP I.

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6

Hartmann, S., S. Augustin, T. Clauss, H. Wex, T. Šantl-Temkiv, J. Voigtländer, D. Niedermeier, and F. Stratmann. "Immersion freezing of ice nucleation active protein complexes." Atmospheric Chemistry and Physics 13, no. 11 (June 14, 2013): 5751–66. http://dx.doi.org/10.5194/acp-13-5751-2013.

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Abstract. Utilising the Leipzig Aerosol Cloud Interaction Simulator (LACIS), the immersion freezing behaviour of droplet ensembles containing monodisperse particles, generated from a Snomax™ solution/suspension, was investigated. Thereto ice fractions were measured in the temperature range between −5 °C to −38 °C. Snomax™ is an industrial product applied for artificial snow production and contains Pseudomonas syringae} bacteria which have long been used as model organism for atmospheric relevant ice nucleation active (INA) bacteria. The ice nucleation activity of such bacteria is controlled by INA protein complexes in their outer membrane. In our experiments, ice fractions increased steeply in the temperature range from about −6 °C to about −10 °C and then levelled off at ice fractions smaller than one. The plateau implies that not all examined droplets contained an INA protein complex. Assuming the INA protein complexes to be Poisson distributed over the investigated droplet populations, we developed the CHESS model (stoCHastic modEl of similar and poiSSon distributed ice nuclei) which allows for the calculation of ice fractions as function of temperature and time for a given nucleation rate. Matching calculated and measured ice fractions, we determined and parameterised the nucleation rate of INA protein complexes exhibiting class III ice nucleation behaviour. Utilising the CHESS model, together with the determined nucleation rate, we compared predictions from the model to experimental data from the literature and found good agreement. We found that (a) the heterogeneous ice nucleation rate expression quantifying the ice nucleation behaviour of the INA protein complex is capable of describing the ice nucleation behaviour observed in various experiments for both, Snomax™ and P. syringae bacteria, (b) the ice nucleation rate, and its temperature dependence, seem to be very similar regardless of whether the INA protein complexes inducing ice nucleation are attached to the outer membrane of intact bacteria or membrane fragments, (c) the temperature range in which heterogeneous droplet freezing occurs, and the fraction of droplets being able to freeze, both depend on the actual number of INA protein complexes present in the droplet ensemble, and (d) possible artifacts suspected to occur in connection with the drop freezing method, i.e., the method frequently used by biologist for quantifying ice nucleation behaviour, are of minor importance, at least for substances such as P. syringae, which induce freezing at comparably high temperatures. The last statement implies that for single ice nucleation entities such as INA protein complexes, it is the number of entities present in the droplet population, and the entities' nucleation rate, which control the freezing behaviour of the droplet population. Quantities such as ice active surface site density are not suitable in this context. The results obtained in this study allow a different perspective on the quantification of the immersion freezing behaviour of bacterial ice nucleation.

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7

Ling, M. L., H. Wex, S. Grawe, J. Jakobsson, J. Löndahl, S. Hartmann, K. Finster, T. Boesen, and T. Šantl‐Temkiv. "Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity." Journal of Geophysical Research: Atmospheres 123, no. 3 (February 12, 2018): 1802–10. http://dx.doi.org/10.1002/2017jd027307.

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8

Sarhan, Mohammed. "Ice nucleation protein as a bacterial surface display protein." Archives of Biological Sciences 63, no. 4 (2011): 943–48. http://dx.doi.org/10.2298/abs1104943s.

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Surface display technology can be defined as that phenotype (protein or peptide) which is linked to a genotype (DNA or RNA) through an appropriate anchoring motif. A bacterial surface display system is based on expressing recombinant proteins fused to sorting signals (anchoring motifs) that direct their incorporation on the cell surface.

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9

Xu, Hao, Marilyn Griffith, Cheryl L. Patten, and Bernard R. Glick. "Isolation and characterization of an antifreeze protein with ice nucleation activity from the plant growth promoting rhizobacterium Pseudomonas putida GR12-2." Canadian Journal of Microbiology 44, no. 1 (January 1, 1998): 64–73. http://dx.doi.org/10.1139/w97-126.

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An antifreeze protein secreted to the growth medium by the plant growth promoting rhizobacterium Pseudomonas putida GR12-2 was purified to apparent homogeneity. The purified protein has a molecular mass of 164 ± 15 kDa and an isoelectric point of 5.3, contains both carbohydrate and lipid moieties, and is relatively rich in glycine and alanine. The properties of the purified antifreeze protein are similar to the properties previously reported for bacterial ice-nucleation proteins. In fact, the purified antifreeze protein also displays a low level of ice-nucleation activity. Removal of approximately 92 kDa of carbohydrate from the 164-kDa antifreeze glycoprotein did not noticeably alter the antifreeze activity of the molecule, although it did diminish the ice-nucleation activity. This is the first report of an antifreeze protein that also is active as an ice-nucleation protein.Key words: antifreeze protein, plant growth promoting rhizobacteria, freezing tolerance, ice-nucleation protein.

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10

Ala, Paul, Pele Chong, Vettai S. Ananthanarayanan, Neville Chan, and Daniel S. C. Yang. "Synthesis and characterization of a fragment of an ice nucleation protein." Biochemistry and Cell Biology 71, no. 5-6 (May 1, 1993): 236–40. http://dx.doi.org/10.1139/o93-036.

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Synthetic peptides were used as models for studying the conformation of ice nucleation proteins. We chemically synthesized four peptides (16-, 24-, 32-, and 48-mer) that consisted of two to six repeats of the consensus repeating octapeptide unit of ice nucleation proteins and evaluated their conformation by circular dichroism spectroscopy. These model peptides exist predominantly as random coils in aqueous solution, but adopt α-helical structures in the presence of trifluoroethanol. The stability of their secondary structures was investigated by monitoring the pH and time dependence of their circular dichroism spectra. Our results indicated that the α-helical content of the 48-mer exhibited a significant pH dependence, while that of the 24- and 32-mer peptides did not. The 32-mer was the only peptide that transformed from the α-helical to a β-sheet structure upon storage. We suggest that the overall conformation of the ice nucleation protein could be a β-sheet.Key words: ice nucleation protein, synthetic peptides, circular dichroism.

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11

Kobashigawa, Yoshihiro, Yoshiyuki Nishimiya, Kazunori Miura, Satoru Ohgiya, Ai Miura, and Sakae Tsuda. "A part of ice nucleation protein exhibits the ice-binding ability." FEBS Letters 579, no. 6 (February 5, 2005): 1493–97. http://dx.doi.org/10.1016/j.febslet.2005.01.056.

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12

Graether, Steffen P., and Zongchao Jia. "Modeling Pseudomonas syringae Ice-Nucleation Protein as aβ-Helical Protein." Biophysical Journal 80, no. 3 (March 2001): 1169–73. http://dx.doi.org/10.1016/s0006-3495(01)76093-6.

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13

Schwidetzky, Ralph, Max Lukas, Azade YazdanYar, Anna T. Kunert, Ulrich Pöschl, Katrin F. Domke, Janine Fröhlich‐Nowoisky, et al. "Specific Ion–Protein Interactions Influence Bacterial Ice Nucleation." Chemistry – A European Journal 27, no. 26 (March 16, 2021): 7402–7. http://dx.doi.org/10.1002/chem.202004630.

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14

Yadollahpour, A., N. A. Bagheri, and H. Rahimian. "INA Gene Inactivation in Isolated Strains from Frozen Leaves and its Effects on Plant Freezing." Cercetari Agronomice in Moldova 49, no. 3 (September 1, 2016): 63–70. http://dx.doi.org/10.1515/cerce-2016-0026.

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Abstract Freezing is a major environmental stress, which limits plant’s distribution, growth and productivity. Ice nucleation active bacteria can catalyze ice formation at temperatures as high as −2°C. A membrane protein confer the ability of ice nucleation, called ice-nucleating proteins (INPs), which is encoded by a single gene. Mutation in this gene will lead to delaying of ice nucleation. In this study, leaf tissues of several plants with freezing symptoms were collected from different locations and 40 bacterial isolates with yellow circular colonies and regular margins were isolated from samples. Finally, total of 12 isolates belong to Xanthomonas were selected for ice nucleate activity (INA) by Droplet-freezing test and presence of INA gene was surveyed by PCR. According to the obtained results, isolate 28 was targeted to mutagenesis by using Tn5 transposon. After mutagenesis, isolates with ability to grow on kanamycin, which lack of INAx gene in PCR were considered as mutated isolates and their freezing effects were evaluated on bean seedlings. Results showed that isolates with mutated INA gene cannot induce freezing on bean seedlings, while primary identified isolate (isolate 28) could do it. These results show that if we could replace wild type ice nucleation active bacteria with mutated forms (just different in ice nucleation activity), we could, probably, prevent freezing and subsequent economic losses.

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15

Steinke, Isabelle, Naruki Hiranuma, Roger Funk, Kristina Höhler, Nadine Tüllmann, Nsikanabasi Silas Umo, Peter G. Weidler, Ottmar Möhler, and Thomas Leisner. "Complex plant-derived organic aerosol as ice-nucleating particles – more than the sums of their parts?" Atmospheric Chemistry and Physics 20, no. 19 (October 6, 2020): 11387–97. http://dx.doi.org/10.5194/acp-20-11387-2020.

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Abstract. Quantifying the impact of complex organic particles on the formation of ice crystals in clouds remains challenging, mostly due to the vast number of different sources ranging from sea spray to agricultural areas. In particular, there are many open questions regarding the ice nucleation properties of organic particles released from terrestrial sources such as decaying plant material. In this work, we present results from laboratory studies investigating the immersion freezing properties of individual organic compounds commonly found in plant tissue and complex organic aerosol particles from vegetated environments, without specifically investigating the contribution from biological particles, which may contribute to the overall ice nucleation efficiency observed at high temperatures. To characterize the ice nucleation properties of plant-related aerosol samples for temperatures between 242 and 267 K, we used the Aerosol Interaction and Dynamics in the Atmosphere (AIDA) cloud chamber and the Ice Nucleation SpEctrometer of the Karlsruhe Institute of Technology (INSEKT), which is a droplet freezing assay. Individual plant components (polysaccharides, lignin, soy and rice protein) were mostly less ice active, or similarly ice active, compared to microcrystalline cellulose, which has been suggested by recent studies to be a proxy for quantifying the primary cloud ice formation caused by particles originating from vegetation. In contrast, samples from ambient sources with a complex organic matter composition (agricultural soils and leaf litter) were either similarly ice active or up to 2 orders of magnitude more ice active than cellulose. Of all individual organic plant components, only carnauba wax (i.e., lipids) showed a similarly high ice nucleation activity as that of the samples from vegetated environments over a temperature range between 245 and 252 K. Hence, based on our experimental results, we suggest considering cellulose as being representative for the average ice nucleation activity of plant-derived particles, whereas lignin and plant proteins tend to provide a lower limit. In contrast, complex biogenic particles may exhibit ice nucleation activities which are up to 2 orders of magnitude higher than observed for cellulose, making ambient plant-derived particles a potentially important contributor to the population of ice-nucleating particles in the troposphere, even though major uncertainties regarding their transport to cloud altitude remain.

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16

Muryoi, Naomi, Mika Sato, Shoji Kaneko, Hidehisa Kawahara, Hitoshi Obata, Mahmoud W. F. Yaish, Marilyn Griffith, and Bernard R. Glick. "Cloning and Expression of afpA, a Gene Encoding an Antifreeze Protein from the Arctic Plant Growth-Promoting Rhizobacterium Pseudomonas putida GR12-2." Journal of Bacteriology 186, no. 17 (September 1, 2004): 5661–71. http://dx.doi.org/10.1128/jb.186.17.5661-5671.2004.

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ABSTRACT The Arctic plant growth-promoting rhizobacterium Pseudomonas putida GR12-2 secretes an antifreeze protein (AFP) that promotes survival at subzero temperatures. The AFP is unusual in that it also exhibits a low level of ice nucleation activity. A DNA fragment with an open reading frame encoding 473 amino acids was cloned by PCR and inverse PCR using primers designed from partial amino acid sequences of the isolated AFP. The predicted gene product, AfpA, had a molecular mass of 47.3 kDa, a pI of 3.51, and no previously known function. Although AfpA is a secreted protein, it lacked an N-terminal signal peptide and was shown by sequence analysis to have two possible secretion systems: a hemolysin-like, calcium-binding secretion domain and a type V autotransporter domain found in gram-negative bacteria. Expression of afpA in Escherichia coli yielded an intracellular 72-kDa protein modified with both sugars and lipids that exhibited lower levels of antifreeze and ice nucleation activities than the native protein. The 164-kDa AFP previously purified from P. putida GR12-2 was a lipoglycoprotein, and the carbohydrate was required for ice nucleation activity. Therefore, the recombinant protein may not have been properly posttranslationally modified. The AfpA sequence was most similar to cell wall-associated proteins and less similar to ice nucleation proteins (INPs). Hydropathy plots revealed that the amino acid sequence of AfpA was more hydrophobic than those of the INPs in the domain that forms the ice template, thus suggesting that AFPs and INPs interact differently with ice. To our knowledge, this is the first gene encoding a protein with both antifreeze and ice nucleation activities to be isolated and characterized.

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Varsaki, Athanasia, Angelos Perisynakis, and Constantin Drainas. "Release of Cell-Free Ice Nucleators from Three Recombinant Ice⁺Zymomonas mobilis Strains." Journal of Molecular Microbiology and Biotechnology 25, no. 4 (2015): 277–83. http://dx.doi.org/10.1159/000433471.

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<b><i>Background/Aims:</i></b> This work is a study of the ability of three recombinant <i>Zymomonas mobilis </i>strains to release ice nucleators into their growth medium. <b><i>Methods:</i></b> The recombinant ice<sup>+</sup><i>Z. mobilis</i> cells were tested for their ability to produce cell-free ice nucleators, under three different growth temperatures and three different glucose concentrations. <b><i>Results:</i></b> Cell-free ice nucleators were obtained from all the recombinant ice<sup>+</sup><i>Z. mobilis</i> cells tested. The cell-free ice nucleation activity was not affected by the glucose concentration in the growth medium or the growth temperature. The freezing temperature threshold was below -7.6°C, demonstrating a class C nucleating structure of the ice nucleation protein. The size of the ice nucleators was less than 0.22 μm and their density was estimated as 1.024 ± 0.004 g/ml by Percoll density centrifugation. The properties of the detected ice nucleators, in addition to the absence of pyruvate decarboxylase activity in the spent medium (a cytosolic marker), support that the cell-free ice nucleation activity was due to the extracellular release of ice nucleators. <b><i>Conclusion:</i></b> These findings indicate that the recombinant ice<sup>+</sup><i>Z. mobilis</i> cells could be valuable for future use as a source of active cell-free ice nucleation protein.

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18

Kumaki, Y., K. Kawano, and N. Matsushima. "1P015 Structure of tandem repeats within ice nucleation protein." Seibutsu Butsuri 45, supplement (2005): S35. http://dx.doi.org/10.2142/biophys.45.s35_3.

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19

Wolber, P. K., C. A. Deininger, M. W. Southworth, J. Vandekerckhove, M. van Montagu, and G. J. Warren. "Identification and purification of a bacterial ice-nucleation protein." Proceedings of the National Academy of Sciences 83, no. 19 (October 1, 1986): 7256–60. http://dx.doi.org/10.1073/pnas.83.19.7256.

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20

Chungjatupornchai, Wipa, and Sirirat Fa-aroonsawat. "Translocation of green fluorescent protein to cyanobacterial periplasm using ice nucleation protein." Journal of Microbiology 47, no. 2 (April 2009): 187–92. http://dx.doi.org/10.1007/s12275-008-0188-x.

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21

Cascajo-Castresana, María, Robert O. David, Maiara A. Iriarte-Alonso, Alexander M. Bittner, and Claudia Marcolli. "Protein aggregates nucleate ice: the example of apoferritin." Atmospheric Chemistry and Physics 20, no. 6 (March 20, 2020): 3291–315. http://dx.doi.org/10.5194/acp-20-3291-2020.

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Abstract. Biological material has gained increasing attention recently as a source of ice-nucleating particles that may account for cloud glaciation at moderate supercooling. While the ice-nucleation (IN) ability of some bacteria can be related to membrane-bound proteins with epitaxial fit to ice, little is known about the IN-active entities present in biological material in general. To elucidate the potential of proteins and viruses to contribute to the IN activity of biological material, we performed bulk freezing experiments with the newly developed drop freezing assay DRoplet Ice Nuclei Counter Zurich (DRINCZ), which allows the simultaneous cooling of 96 sample aliquots in a chilled ethanol bath. We performed a screening of common proteins, namely the iron storage protein ferritin and its iron-free counterpart apoferritin, the milk protein casein, the egg protein ovalbumin, two hydrophobins, and a yeast ice-binding protein, all of which revealed IN activity with active site densities > 0.1 mg−1 at −10 ∘C. The tobacco mosaic virus, a plant virus based on helically assembled proteins, also proved to be IN active with active site densities increasing from 100 mg−1 at −14 ∘C to 10 000 mg−1 at −20 ∘C. Among the screened proteins, the IN activity of horse spleen ferritin and apoferritin, which form cages of 24 co-assembled protein subunits, proved to be outstanding with active site densities > 10 mg−1 at −5 ∘C. Investigation of the pH dependence and heat resistance of the apoferritin sample confirmed the proteinaceous nature of its IN-active entities but excluded the correctly folded cage monomer as the IN-active species. A dilution series of apoferritin in water revealed two distinct freezing ranges, an upper one from −4 to −11 ∘C and a lower one from −11 to −21 ∘C. Dynamic light scattering measurements related the upper freezing range to ice-nucleating sites residing on aggregates and the lower freezing range to sites located on misfolded cage monomers or oligomers. The sites proved to persist during several freeze–thaw cycles performed with the same sample aliquots. Based on these results, IN activity seems to be a common feature of diverse proteins, irrespective of their function, but arising only rarely, most probably through defective folding or aggregation to structures that are IN active.

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Shimazu, M., A. Mulchandani, and W. Chen. "Cell Surface Display of Organophosphorus Hydrolase Using Ice Nucleation Protein." Biotechnology Progress 17, no. 1 (February 2, 2001): 76–80. http://dx.doi.org/10.1021/bp0001563.

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Luoma, Jacob, Erika Ingham, Carmen Lema Martinez, and Andrea Allmendinger. "Comparison of Techniques to Control Ice Nucleation during Lyophilization." Processes 8, no. 11 (November 11, 2020): 1439. http://dx.doi.org/10.3390/pr8111439.

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Controlling ice nucleation during lyophilization of parenteral drug products increases the homogeneity of critical quality attributes, such as residual moisture, across drug product batches and shortens lyophilization cycle time. In the present study, we compare three mechanistically different techniques to control ice nucleation during the freezing step of lyophilization, which are referred to as “depressurization”, “partial vacuum”, and “ice fog” techniques. The techniques are compared with respect to their operational limitations and challenges. Installation considerations are also discussed. Using the aforementioned nucleation techniques, we investigated a monoclonal antibody formulation and an enzyme formulation at different protein concentrations using feasible nucleation temperatures and different vial formats and fill volumes. Samples were compared for solid state properties and other critical quality attributes on stability. When nucleated at the same temperature, the three techniques produced products with the same quality attributes and stability behavior. Under conditions resulting in micro-collapse, stability behavior can be different. We found that each technology had considerations for achieving robust nucleation. The present comparison may serve as guidance in selecting a nucleation method.

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Kwak, Young-Don, Seung-Ku Yoo, and Eui-Joong Kim. "Cell Surface Display of Human Immunodeficiency Virus Type 1 gp120 on Escherichia coli by Using Ice Nucleation Protein." Clinical Diagnostic Laboratory Immunology 6, no. 4 (July 1, 1999): 499–503. http://dx.doi.org/10.1128/cdli.6.4.499-503.1999.

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ABSTRACT A new system designed for cell surface display of recombinant proteins on Escherichia coli has been evaluated for expression of eukaryotic viral proteins. Human immunodeficiency virus type 1 (HIV-1) gp120 was fused to the C terminus of ice nucleation protein (INP), an outer membrane protein of Pseudomonas syringae. Western blotting, immunofluorescence microscopy, fluorescence-activated cell-sorting analysis, whole-cell enzyme-linked immunosorbent assay, and ice nucleation activity assay confirmed the successful expression of HIV-1 gp120 on the surface ofEscherichia coli. This study shows that the INP system can be used for the expression of eukaryotic viral proteins. There is also a possibility that the INP system can be used as an AIDS diagnostic system, an oral vaccine delivery system, and an expression system for various heterologous higher-molecular-weight proteins.

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Kassmannhuber, Johannes, Sergio Mauri, Mascha Rauscher, Nadja Brait, Lea Schöner, Angela Witte, Tobias Weidner, and Werner Lubitz. "Freezing from the inside: Ice nucleation in Escherichia coli and Escherichia coli ghosts by inner membrane bound ice nucleation protein InaZ." Biointerphases 15, no. 3 (May 2020): 031003. http://dx.doi.org/10.1116/1.5142174.

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26

Schmid, Daniel, David Pridmore, Guido Capitani, Roberto Battistutta, Jean-Richard Neeser, and Alfred Jann. "Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae." FEBS Letters 414, no. 3 (September 15, 1997): 590–94. http://dx.doi.org/10.1016/s0014-5793(97)01079-x.

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27

Du, Ning, and Xiang Y. Liu. "Enhanced Antifreeze Effect of Antifreeze Protein on Ice Nucleation by Electrolyte." Crystal Growth & Design 8, no. 9 (September 3, 2008): 3290–94. http://dx.doi.org/10.1021/cg800118z.

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28

Tomalty, Heather E., and Virginia K. Walker. "Perturbation of bacterial ice nucleation activity by a grass antifreeze protein." Biochemical and Biophysical Research Communications 452, no. 3 (September 2014): 636–41. http://dx.doi.org/10.1016/j.bbrc.2014.08.138.

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29

Han, Yu Jin, HyoJin Song, Chang Woo Lee, Nguyễn Hoàng Ly, Sang-Woo Joo, Jun Hyuck Lee, Soon-Jong Kim, and SangYoun Park. "Biophysical characterization of soluble Pseudomonas syringae ice nucleation protein InaZ fragments." International Journal of Biological Macromolecules 94 (January 2017): 634–41. http://dx.doi.org/10.1016/j.ijbiomac.2016.10.062.

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30

Wu, Zhongqin, Lei Qin, and Virginia K. Walker. "Characterization and recombinant expression of a divergent ice nucleation protein from ‘Pseudomonas borealis’." Microbiology 155, no. 4 (April 1, 2009): 1164–69. http://dx.doi.org/10.1099/mic.0.025114-0.

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Isolates of ‘Pseudomonas borealis’ were recovered after ice-affinity selection of summer-collected soils. ‘P. borealis’ DL7 was further characterized and shown to have ice nucleation activity (INA), a property that allows the crystallization of ice at temperatures close to the melting point, effectively preventing the supercooling of water. INA was optimally detected after culturing at temperatures consistent with psychrophilic growth. The sequence encoding the ‘P. borealis’ ice nucleation protein (INP) was obtained using both PCR and chromosome walking. When expressed in Escherichia coli, the resulting inaPb recombinants had INA. The ‘P. borealis’ sequence, dubbed inaPb, is clearly related to previously cloned INP genes, but it shows greater divergence. Sequence analysis suggests that there are two opposite flat surfaces, one relatively hydrophobic that likely serves as an ice template, and the other that could function as a complementary face to facilitate interprotein interaction for ice-step formation.

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Roy, Priyatanu, Margaret House, and Cari Dutcher. "A Microfluidic Device for Automated High Throughput Detection of Ice Nucleation of Snomax®." Micromachines 12, no. 3 (March 11, 2021): 296. http://dx.doi.org/10.3390/mi12030296.

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Measurement of ice nucleation (IN) temperature of liquid solutions at sub-ambient temperatures has applications in atmospheric, water quality, food storage, protein crystallography and pharmaceutical sciences. Here we present details on the construction of a temperature-controlled microfluidic platform with multiple individually addressable temperature zones and on-chip temperature sensors for high-throughput IN studies in droplets. We developed, for the first time, automated droplet freezing detection methods in a microfluidic device, using a deep neural network (DNN) and a polarized optical method based on intensity thresholding to classify droplets without manual counting. This platform has potential applications in continuous monitoring of liquid samples consisting of aerosols to quantify their IN behavior, or in checking for contaminants in pure water. A case study of the two detection methods was performed using Snomax® (Snomax International, Englewood, CO, USA), an ideal ice nucleating particle (INP). Effects of aging and heat treatment of Snomax® were studied with Fourier transform infrared (FTIR) spectroscopy and a microfluidic platform to correlate secondary structure change of the IN protein in Snomax® to IN temperature. It was found that aging at room temperature had a mild impact on the ice nucleation ability but heat treatment at 95 °C had a more pronounced effect by reducing the ice nucleation onset temperature by more than 7 °C and flattening the overall frozen fraction curve. Results also demonstrated that our setup can generate droplets at a rate of about 1500/min and requires minimal human intervention for DNN classification.

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Allmendinger, Andrea, Yuen Li Butt, Raphael Mietzner, Felix Schmidt, Joerg Luemkemann, and Carmen Lema Martinez. "Controlling Ice Nucleation during Lyophilization: Process Optimization of Vacuum-Induced Surface Freezing." Processes 8, no. 10 (October 8, 2020): 1263. http://dx.doi.org/10.3390/pr8101263.

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Biopharmaceuticals are often lyophilized to improve their storage stability. Controlling ice nucleation during the freezing step of the lyophilization process is desired to increase homogeneity of product properties across a drug product batch and shorten the primary drying time. The present communication summarizes the process optimization of the freezing process when using vacuum-induced surface freezing to control ice nucleation, in particular for amorphous samples. We characterized freeze-dried samples for solid state properties, and compared these to uncontrolled nucleated samples using bovine serum albumin (BSA) as a model protein. Freezing parameters were optimized to obtain complete nucleation, adequate cake resistance during the subsequent lyophilization cycle, and elegant cakes. We highlight the challenges associated with vacuum-induced surface freezing and propose optimized freezing parameters to control ice nucleation, enabling manufacturing of amorphous samples.

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Hill, Tom C. J., Paul J. DeMott, Yutaka Tobo, Janine Fröhlich-Nowoisky, Bruce F. Moffett, Gary D. Franc, and Sonia M. Kreidenweis. "Sources of organic ice nucleating particles in soils." Atmospheric Chemistry and Physics 16, no. 11 (June 10, 2016): 7195–211. http://dx.doi.org/10.5194/acp-16-7195-2016.

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Abstract. Soil organic matter (SOM) may be a significant source of atmospheric ice nucleating particles (INPs), especially of those active > −15 °C. However, due to both a lack of investigations and the complexity of the SOM itself, the identities of these INPs remain unknown. To more comprehensively characterize organic INPs we tested locally representative soils in Wyoming and Colorado for total organic INPs, INPs in the heat-labile fraction, ice nucleating (IN) bacteria, IN fungi, IN fulvic and humic acids, IN plant tissue, and ice nucleation by monolayers of aliphatic alcohols. All soils contained ≈ 106 to ≈ 5 × 107 INPs g−1 dry soil active at −10 °C. Removal of SOM with H2O2 removed ≥ 99 % of INPs active > −18 °C (the limit of testing), while heating of soil suspensions to 105 °C showed that labile INPs increasingly predominated > −12 °C and comprised ≥ 90 % of INPs active > −9 °C. Papain protease, which inactivates IN proteins produced by the fungus Mortierella alpina, common in the region's soils, lowered INPs active at ≥ −11 °C by ≥ 75 % in two arable soils and in sagebrush shrubland soil. By contrast, lysozyme, which digests bacterial cell walls, only reduced INPs active at ≥ −7.5 or ≥ −6 °C, depending on the soil. The known IN bacteria were not detected in any soil, using PCR for the ina gene that codes for the active protein. We directly isolated and photographed two INPs from soil, using repeated cycles of freeze testing and subdivision of droplets of dilute soil suspensions; they were complex and apparently organic entities. Ice nucleation activity was not affected by digestion of Proteinase K-susceptible proteins or the removal of entities composed of fulvic and humic acids, sterols, or aliphatic alcohol monolayers. Organic INPs active colder than −10 to −12 °C were resistant to all investigations other than heat, oxidation with H2O2, and, for some, digestion with papain. They may originate from decomposing plant material, microbial biomass, and/or the humin component of the SOM. In the case of the latter then they are most likely to be a carbohydrate. Reflecting the diversity of the SOM itself, soil INPs have a range of sources which occur with differing relative abundances.

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HU, JIN, OSMANN SARI, and CYRIL MAHMED. "IMPROVING ICE FORMATION BY ADDITIVE FOR COLD ENERGY STORAGE." International Journal of Air-Conditioning and Refrigeration 22, no. 03 (September 2014): 1450012. http://dx.doi.org/10.1142/s2010132514500126.

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Ice storage is one technique for effective use of thermal energy. Application of bionucleant (a protein from the bacterium Pseudomonas syringae) as a snow inducer in ski field has shown great potential to enhance the quantity of snow and increase freezing temperature. In this study, differential scanning calorimeter (DSC) and lab-built ice formation reactor were employed to study experimentally the heterogeneous ice nucleation under super-cooled conditions at different dissolved bionucleant concentrations. It was found the degree of supercooling is reduced by addition of bionucleant. However, ice nucleation-activity of bionucleant will drop down when bionucleant solution is saturated/supersaturated. In our DSC measured heat release study, when bionucleant acts as ice nucleation agent in aqueous solution, prior to reaching its saturation/supersaturation, there is an increase in latent heat release during freezing/melting as the amount of dissolved bionucleant increases. In another test, the supercooling does not occur in 0.5% bionucleant solution, it began to freeze around 0°C. Our results suggest that, the addition of bionucleant may help induce ice nucleation and increase freezing temperature thereby reduces the energy consumption of ice formation for cold storage.

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Watabe, Satoshi, Keiko Abe, Aiko Hirata, Yasufumi Emori, Michiko Watanabe, and Soichi Arai. "Large-scale Production and Purification of anErwinia ananasIce Nucleation Protein and Evaluation of Its Ice Nucleation Activity." Bioscience, Biotechnology, and Biochemistry 57, no. 4 (January 1993): 603–6. http://dx.doi.org/10.1271/bbb.57.603.

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Southworth, M. W., P. K. Wolber, and G. J. Warren. "Nonlinear relationship between concentration and activity of a bacterial ice nucleation protein." Journal of Biological Chemistry 263, no. 29 (October 1988): 15211–16. http://dx.doi.org/10.1016/s0021-9258(18)68166-9.

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Mizuno, Hiroshige. "Prediction of the conformation of ice-nucleation protein by conformational energy calculation." Proteins: Structure, Function, and Genetics 5, no. 1 (1989): 47–65. http://dx.doi.org/10.1002/prot.340050107.

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Geidobler, Raimund, Ilona Konrad, and Gerhard Winter. "Can Controlled Ice Nucleation Improve Freeze‐Drying of Highly‐Concentrated Protein Formulations?" Journal of Pharmaceutical Sciences 102, no. 11 (November 2013): 3915–19. http://dx.doi.org/10.1002/jps.23704.

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Li, Qianqian, Ziniu Yu, Xiaohu Shao, Jin He, and Lin Li. "Improved phosphate biosorption by bacterial surface display of phosphate-binding protein utilizing ice nucleation protein." FEMS Microbiology Letters 299, no. 1 (October 2009): 44–52. http://dx.doi.org/10.1111/j.1574-6968.2009.01724.x.

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Moreau, David W., Hakan Atakisi, and Robert E. Thorne. "Ice formation and solvent nanoconfinement in protein crystals." IUCrJ 6, no. 3 (March 13, 2019): 346–56. http://dx.doi.org/10.1107/s2052252519001878.

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Ice formation within protein crystals is a major obstacle to the cryocrystallographic study of protein structure, and has limited studies of how the structural ensemble of a protein evolves with temperature in the biophysically interesting range from ∼260 K to the protein–solvent glass transition near 200 K. Using protein crystals with solvent cavities as large as ∼70 Å, time-resolved X-ray diffraction was used to study the response of protein and internal solvent during rapid cooling. Solvent nanoconfinement suppresses freezing temperatures and ice-nucleation rates so that ice-free, low-mosaicity diffraction data can be reliably collected down to 200 K without the use of cryoprotectants. Hexagonal ice (Ih) forms in external solvent, but internal crystal solvent forms stacking-disordered ice (Isd) with a near-random stacking of cubic and hexagonal planes. Analysis of powder diffraction from internal ice and single-crystal diffraction from the host protein structure shows that the maximum crystallizable solvent fraction decreases with decreasing crystal solvent-cavity size, and that an ∼6 Å thick layer of solvent adjacent to the protein surface cannot crystallize. These results establish protein crystals as excellent model systems for the study of nanoconfined solvent. By combining fast cooling, intense X-ray beams and fast X-ray detectors, complete structural data sets for high-value targets, including membrane proteins and large complexes, may be collected at ∼220–240 K that have much lower mosaicities and comparableBfactors, and that may allow more confident identification of ligand binding than in current cryocrystallographic practice.

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DeMott, Paul J., Ottmar Möhler, Daniel J. Cziczo, Naruki Hiranuma, Markus D. Petters, Sarah S. Petters, Franco Belosi, et al. "The Fifth International Workshop on Ice Nucleation phase 2 (FIN-02): laboratory intercomparison of ice nucleation measurements." Atmospheric Measurement Techniques 11, no. 11 (November 19, 2018): 6231–57. http://dx.doi.org/10.5194/amt-11-6231-2018.

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Abstract. The second phase of the Fifth International Ice Nucleation Workshop (FIN-02) involved the gathering of a large number of researchers at the Karlsruhe Institute of Technology's Aerosol Interactions and Dynamics of the Atmosphere (AIDA) facility to promote characterization and understanding of ice nucleation measurements made by a variety of methods used worldwide. Compared to the previous workshop in 2007, participation was doubled, reflecting a vibrant research area. Experimental methods involved sampling of aerosol particles by direct processing ice nucleation measuring systems from the same volume of air in separate experiments using different ice nucleating particle (INP) types, and collections of aerosol particle samples onto filters or into liquid for sharing amongst measurement techniques that post-process these samples. In this manner, any errors introduced by differences in generation methods when samples are shared across laboratories were mitigated. Furthermore, as much as possible, aerosol particle size distribution was controlled so that the size limitations of different methods were minimized. The results presented here use data from the workshop to assess the comparability of immersion freezing measurement methods activating INPs in bulk suspensions, methods that activate INPs in condensation and/or immersion freezing modes as single particles on a substrate, continuous flow diffusion chambers (CFDCs) directly sampling and processing particles well above water saturation to maximize immersion and subsequent freezing of aerosol particles, and expansion cloud chamber simulations in which liquid cloud droplets were first activated on aerosol particles prior to freezing. The AIDA expansion chamber measurements are expected to be the closest representation to INP activation in atmospheric cloud parcels in these comparisons, due to exposing particles freely to adiabatic cooling. The different particle types used as INPs included the minerals illite NX and potassium feldspar (K-feldspar), two natural soil dusts representative of arable sandy loam (Argentina) and highly erodible sandy dryland (Tunisia) soils, respectively, and a bacterial INP (Snomax®). Considered together, the agreement among post-processed immersion freezing measurements of the numbers and fractions of particles active at different temperatures following bulk collection of particles into liquid was excellent, with possible temperature uncertainties inferred to be a key factor in determining INP uncertainties. Collection onto filters for rinsing versus directly into liquid in impingers made little difference. For methods that activated collected single particles on a substrate at a controlled humidity at or above water saturation, agreement with immersion freezing methods was good in most cases, but was biased low in a few others for reasons that have not been resolved, but could relate to water vapor competition effects. Amongst CFDC-style instruments, various factors requiring (variable) higher supersaturations to achieve equivalent immersion freezing activation dominate the uncertainty between these measurements, and for comparison with bulk immersion freezing methods. When operated above water saturation to include assessment of immersion freezing, CFDC measurements often measured at or above the upper bound of immersion freezing device measurements, but often underestimated INP concentration in comparison to an immersion freezing method that first activates all particles into liquid droplets prior to cooling (the PIMCA-PINC device, or Portable Immersion Mode Cooling chAmber–Portable Ice Nucleation Chamber), and typically slightly underestimated INP number concentrations in comparison to cloud parcel expansions in the AIDA chamber; this can be largely mitigated when it is possible to raise the relative humidity to sufficiently high values in the CFDCs, although this is not always possible operationally. Correspondence of measurements of INPs among direct sampling and post-processing systems varied depending on the INP type. Agreement was best for Snomax® particles in the temperature regime colder than −10 ∘C, where their ice nucleation activity is nearly maximized and changes very little with temperature. At temperatures warmer than −10 ∘C, Snomax® INP measurements (all via freezing of suspensions) demonstrated discrepancies consistent with previous reports of the instability of its protein aggregates that appear to make it less suitable as a calibration INP at these temperatures. For Argentinian soil dust particles, there was excellent agreement across all measurement methods; measures ranged within 1 order of magnitude for INP number concentrations, active fractions and calculated active site densities over a 25 to 30 ∘C range and 5 to 8 orders of corresponding magnitude change in number concentrations. This was also the case for all temperatures warmer than −25 ∘C in Tunisian dust experiments. In contrast, discrepancies in measurements of INP concentrations or active site densities that exceeded 2 orders of magnitude across a broad range of temperature measurements found at temperatures warmer than −25 ∘C in a previous study were replicated for illite NX. Discrepancies also exceeded 2 orders of magnitude at temperatures of −20 to −25 ∘C for potassium feldspar (K-feldspar), but these coincided with the range of temperatures at which INP concentrations increase rapidly at approximately an order of magnitude per 2 ∘C cooling for K-feldspar. These few discrepancies did not outweigh the overall positive outcomes of the workshop activity, nor the future utility of this data set or future similar efforts for resolving remaining measurement issues. Measurements of the same materials were repeatable over the time of the workshop and demonstrated strong consistency with prior studies, as reflected by agreement of data broadly with parameterizations of different specific or general (e.g., soil dust) aerosol types. The divergent measurements of the INP activity of illite NX by direct versus post-processing methods were not repeated for other particle types, and the Snomax® data demonstrated that, at least for a biological INP type, there is no expected measurement bias between bulk collection and direct immediately processed freezing methods to as warm as −10 ∘C. Since particle size ranges were limited for this workshop, it can be expected that for atmospheric populations of INPs, measurement discrepancies will appear due to the different capabilities of methods for sampling the full aerosol size distribution, or due to limitations on achieving sufficient water supersaturations to fully capture immersion freezing in direct processing instruments. Overall, this workshop presents an improved picture of present capabilities for measuring INPs than in past workshops, and provides direction toward addressing remaining measurement issues.

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42

Missa, Hildegardis, and Anselmus Boy Baunsele. "ISOLASI DAN IDENTIFIKASI POPULASI BAKTERI ICE NUCLEATION ACTIVE PADA JERUK KEPROK SOE DI DATARAN TINGGI MUTIS PROVINSI NUSA TENGGARA TIMUR." Sebatik 23, no. 2 (December 1, 2019): 403–7. http://dx.doi.org/10.46984/sebatik.v23i2.790.

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pada Jeruk Keprok Soe di dataran tinggi Mutis ini akan memberikan informasi kebaruan bakteri INA di daerah tropis. Penelitian lanjut mengenai bakteri INA perlu dilakukan, mengingat dampak buruk bagi pertanian akibat luka beku yang disebabkan karena aktivitas ice nucleation. Tujuan dari penelitian ini adalah untuk mengetahui populasi bakteri INA, mengetahui estimasi populasi bakteri INA, uji aktivitas ice Nucleation Active dan mengetahui kelas protein INA. Pengambilan sampel tanaman Jeruk Keprok Soe menggunakan metode purposive sampling pada tiga ketinggian yaitu 2000, 2100, dan 2200 m dpl. Isolasi bakteri dilakukan dengan metode spread plate pada media Kings’B, aktivitas nukleasi es ditentukan dengan metode tube nucleation test. Estimasi populasi bakteri INA dilakukan dengan metode multiple-tube nucleation test formula Thomas seri 3.3.3. Hasil penelitian menunjukan bahwa populasi bakteri INA yang ditemukan pada daun jeruk keprok soe di dataran tinggi mutis tergolong tinggi yaitu 6 x 103/g hingga 1,2 x 104 /g daun. hal ini menunjukkan bahwa semakin tinggi tempat maka semakin tinggi populasi bakteri INA yang ditemukan. Berdasarkan suhu pembentukan es, terdapat dua isolat bakteri , yaitu 2 sampel mengalami pembekuan pada suhu -7oC dengan kelas protein INA B, sedangkan 6 sampel membeku pada suhu -10oC dengan kelas protein INA C.

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FUNAKI, Junko, Yasuyuki MICHIGAMI, Midori YANO, Atsushi SHIRAISHI, Keiko ABE, and Soichi ARAI. "Applying a Bacterial Ice Nucleation-Active Protein to Preparation of Frozen Bread Dough." NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI 43, no. 7 (1996): 835–38. http://dx.doi.org/10.3136/nskkk.43.835.

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Murakami, Daisuke, and Kenji Yasuoka. "Molecular dynamics simulation of quasi-two-dimensional water clusters on ice nucleation protein." Journal of Chemical Physics 137, no. 5 (August 7, 2012): 054303. http://dx.doi.org/10.1063/1.4739299.

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Kassmannhuber, Johannes, Mascha Rauscher, Lea Schöner, Angela Witte, and Werner Lubitz. "Functional display of ice nucleation protein InaZ on the surface of bacterial ghosts." Bioengineered 8, no. 5 (January 25, 2017): 488–500. http://dx.doi.org/10.1080/21655979.2017.1284712.

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Murakami, Daisuke, and Kenji Yasuoka. "Dependency of Percolation Threshold of Water Cluster on Flexibility of Ice Nucleation Protein." Biophysical Journal 104, no. 2 (January 2013): 172a. http://dx.doi.org/10.1016/j.bpj.2012.11.970.

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47

Kumaki, Yasuhiro, Keiichi Kawano, Kunio Hikichi, Takeshi Matsumoto, and Norio Matsushima. "A circular loop of the 16-residue repeating unit in ice nucleation protein." Biochemical and Biophysical Research Communications 371, no. 1 (June 2008): 5–9. http://dx.doi.org/10.1016/j.bbrc.2008.03.069.

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Li, Lin, Dong Gyun Kang, and Hyung Joon Cha. "Functional display of foreign protein on surface ofEscherichia coli using N-terminal domain of ice nucleation protein." Biotechnology and Bioengineering 85, no. 2 (2003): 214–21. http://dx.doi.org/10.1002/bit.10892.

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49

Pummer, B. G., L. Atanasova, H. Bauer, J. Bernardi, I. S. Druzhinina, and H. Grothe. "Spores of most common airborne fungi reveal no ice nucleation activity." Biogeosciences Discussions 10, no. 6 (June 20, 2013): 10125–41. http://dx.doi.org/10.5194/bgd-10-10125-2013.

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Abstract. Fungal spores are ubiquitous biological aerosols, which are considered to show ice nucleation (IN) activity. In this study the respective IN activity was tested in oil emulsion in the immersion freezing mode. The focus was laid on species of economical, ecological or sanitary significance. For the first time, not only common moulds, but also edible mushrooms (Basidiomycota, Agaricomycetes) were investigated, as they contribute massively to the total amount of fungal spores in the atmosphere. Only Fusarium avenaceum showed freezing events at low subzero-temperatures, while the other investigated fungal spores showed no significant IN activity. Furthermore, we selected a set of fungal strains from different sites and exposed them to occasional freezing stress during cultivation. Although the total protein expression was altered by this treatment, it had no significant impact on the IN activity.

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Cochran, Teresa, and Steven L. Nail. "Ice nucleation temperature influences recovery of activity of a model protein after freeze drying." Journal of Pharmaceutical Sciences 98, no. 9 (September 2009): 3495–98. http://dx.doi.org/10.1002/jps.21815.

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