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Journal articles on the topic "Ice nucleation protein"
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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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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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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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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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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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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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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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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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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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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.
Dissertations / Theses on the topic "Ice nucleation protein"
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Ding, Daniel N. "Membrane display of a fusion protein containing the ice-nucleation protein from Pseudomonas syringae and ScFv against c-myc oncoprotein in recombinant Escherichia coli." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape8/PQDD_0001/MQ42060.pdf.
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Geidobler, Raimund. "Cyclodextrins as excipients in drying of proteins and controlled ice nucleation in freeze-drying." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-167191.
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Geidobler, Raimund [Verfasser], and Gerhard [Akademischer Betreuer] Winter. "Cyclodextrins as excipients in drying of proteins and controlled ice nucleation in freeze-drying / Raimund Geidobler. Betreuer: Gerhard Winter." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1048522466/34.
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WU, ZHONGQIN. "Bacterial low temperature survival, ice nucleation proteins and ice-associating polymers." Thesis, 2010. http://hdl.handle.net/1974/5411.
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Microorganisms have developed ways to preserve cellular functions under low temperature conditions using a variety of biochemical adaptations including the modification of ice formation. In order to conduct a limited survey of microbial ice-associating strategies, a bacterial community associated with frost-exposed leaves was assessed by the construction of a 16S rDNA library, followed by the characterization of some isolates. Fifteen different species were identified based on their 16S rDNA. Among these, Pseudomonas syringae J6 had ice nucleation activity (INA), which promoted ice formation close to 0ºC, whereas Erwinia billingiae, Flavobacterium sp. and Sphingobacterium kitahiroshimense inhibited the recrystallization of small ice crystals at temperatures close to melting. The Erwinia billingiae isolate showed adhesive and swarming behaviour, which can be associated with biofilm formation. Visualization using negative staining, transmission electron microscopy and scanning electron microscopy confirmed the presence of flagella in addition to the presence of slimy biofilm architecture in these Erwina billingiae cultures. Subsequent purification of the extracellular polymeric substance followed by mass spectrometry allowed the identification of a putative outer membrane protein A, which may be involved in the protection of this bacterium to freeze-thaw cycles.
To further explore bacterial ice nucleation activity, an ice nucleation protein was cloned from Pseudomonas borealis, a bacterium originating from tundra soil, using degenerative PCR and chromosome walking. The sequence of the putative ice nucleation protein gene (inaPb) was cloned and expressed in Escherichia coli, and its identification was confirmed in the recombinant cells. Although the INPPb was more divergent than other plant-related bacterial INPs, it retained the highly conserved, repetitive core region. The protein may fold so that it has two flat faces, one for protein-protein interactions and the other for ice binding. Expression of the INPPb coding region fused to jelly fish green fluorescent protein showed a temperature-dependent polarized distribution of the recombinant protein in E. coli.
In summary, results from this thesis suggests that low temperature survival may be associated with a number of ice-associating adaptations including the presence of biofilm formation in Erwina billingiae amongst other bacteria, INA in P. borealis and INA-expressing recombinant E. coli.Thesis (Ph.D, Biology) -- Queen's University, 2010-01-27 11:47:02.385
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Hung, Hsiang-Chia, and 洪祥嘉. "Effect of extracellular ice nucleation protein and cellulose on the nucleation temperature of supercooled liquid." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/24581107565415567866.
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碩士國立臺灣大學
食品科技研究所
99
Ice nucleation active (INA) bacteria are known to be the most active ice nucleator (IN) found in nature to date. However, nearly all INA bacteria are plant-pathogenic or enterobacteriaceae, thus direct applications to food industry are limited. In this research, we utilize extracellular ice nucleator protein (ECIN) as an IN and immobilize it onto a polyethylene (PE) film by employing layer by layer deposition method to minimize direct contact with foods. In addition, we explore the possibility of media-milled cellulose as a replacer of ECIN. Coating ECIN on PE film resulted in freezing of 20% sucrose solution at -8℃, which does not freeze at normal conditions, and reduced 47.2% total freezing time of milk (from 94.6 min to 49.9 min). This film also can reduce the deterioration of fish actomyosin (AM) caused by freeze-thaw cycles during storage. The retention values for the three freeze-thaw cycles were greatly improved from 38%, 21%, 19% to 55%, 33%, 31%. The nucleation temperature of pure water was raised from -21.7℃ to -16.6℃ while cellulose was add. The addition of 5 min media-milled cellulose further raise the nucleation temperature to -13.0℃. Nevertheless, increasing milling did not further raise the nucleation temperature. For examples, 90 min milling resulted in smaller particle size (1.4 μm), but a nucleation temperature at -16.1℃. Our data show that ECIN can reduce the degree of supercooling, total freezing time and preserve the quality of AM even being immobilized onto PE film. Nevertheless, ECIN still have the possible to contact into foods. So, cellulose have the possibility as a replacer of ECIN.
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Tsai, Chun-Yung, and 蔡俊勇. "Expression of Chi92 on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/51545643491523602800.
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碩士國立屏東科技大學
生物科技研究所
92
Recently, several surface anchoring systems have been developed for anchoring heterologous protein on the surface of microorganisms. In bacteria, surface expression system have been reported basically using a surface protein of the cells as an expression motif. The ice-nucleation protein (INP), an outer membrane protein from Pseudomonas syringae, is able to catalyze the ice crystal formation of supercooled water. INP deleted of the repeating domain, thus producing no ice-nucleation activity, could also direct heterologous proteins on the cell surface. This suggests that it has the secretion and targeting signal to the outer membrane. The Chi92 gene was in-frame subcloned for making INP-Chi92 fusion protein and exploited for anchoring Chi92 on the surface of Escherichia coli. JM109 (pNMChi92) was incubated at 30℃ in LB medium and induced by IPTG for 24 hrs. The chitinase activity of washed whole cells is 21.24 mU ml-1. 62 % of total chitinase activity was present on cell surface. The INP-Chi92 fusion protein was confirmed by Western blotting analysis. The surface location of Chi92 was further verified by immunofluorescence microscopy.
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Wu, Jiun-Yan, and 吳俊彥. "Production of recombinant enhanced green fluorescence protein via surface display system of ice nucleation protein coupling with self-cleavage intein." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/9ueta3.
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博士國立中興大學
化學工程學系所
100
Protein production and purification is often costly and laborious due to the complicated processes. It is highly expected to develop a simple process to obtain high purity protein without the complicate purification steps and costly equipments. In this study, a novel recombinant protein production system was developed by using cell surface display segment to finally produce a model protein entity. The system is constructing a fusion protein with a self-cleavage intein along with a cell membrane motife, ice nucleation protein, and a model protein, enhanced green fluorescence protein (EGFP). By using this system, the target protein (here is EGFP in this case) can be separated from the cell membrane by the auto-proteolysis property of intein. The protein production can be obtained in the supernatant by only several centrifugations, no complicate processes or expensive equipments are required. . By simply holding the cell pellets in Tris-HCl (pH 11) with 0.1% (w/v) NaCl buffer at 37℃, EGFP was solubilized from the INP-INT segment embedded on the cell surface via intein’s self-cleavage function. The EGFP concentration of 278 mg/L with the purity of 50% was obtained at day 5. The EGFP can be harvested only via centrifugation, and no cell disruption process is required. Cell membrane damage is helpful for EGFP release in neutral condition. By adding 0.5% Triton X-100 in the cleavage buffer (20 mM Tris–HCl, 1 mM EDTA and 1% NaCl) of pH 8, the EGFP was obtained 184 mg/L with the purity of 27% after reaction for 1 day, and the recovery was 85%. Purity of EGFP production can be increased to 65% by replacing cell pellet into clean cleavage buffer (pH 8) after Triton X-100 pretreatment for 1h, and EGFP production was 40 mg/L with the recovery of 19%. Cell membrane can also be damaged by osmotic shock. In the process of osmotic shock, cells were treated with a concentrated solution of sucrose and then shifted to water, and the impurities in cell periplasm were washed out by the water, followed by shifting the cells into the cleavage buffer (pH 8), EGFP production was 198 mg/L with the recovery of 91% and the purity of 60%. On the other hand, when applying cell disruption in the process, EGFP of 63 mg/L with the purity of 97% and the recovery of 29% was obtained. This study discloses a facile approach producing recombinant protein. Due to the simplicity of the approach, the protein production and purification can be simultaneously carried out in few steps, which might help its realiation in the scale up process. This approach is expected to be an alternative way for recombinant protein production in bio-industry for academic and industrial use.
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Wu, Po-Hung, and 吳柏宏. "Development of a Surface Expression System with the Ice Nucleation Protein and Its Applications in Hydroquinone Glucosylation." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/95403387225143125164.
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博士國立清華大學
化學工程學系
96
A surface anchoring motif using the ice nucleation protein (INP) of Xanthomonas campestris pv. campestris BCRC 12846 for displaying transglucosidase was developed. The transglucosidase gene from Xanthomonas campestris pv. campestris BCRC 12608 was fused to the truncated ina gene. This truncated INP consisting of N- and C-terminal domains (INPNC) was able to direct the expression of transglucosidase fusion protein to the cell surface of E. coli. Localization of the truncated INPNC-transglucosidase fusion protein was examined by Western blot analysis and immunofluorescence labeling, and by whole-cell enzyme activity in the glucosylation of hydroquinone. The glucosylation reaction was carried out at 40℃ for 1 h, which gave 23 g/L of alpha-arbutin, and the molar conversion based on the amount of hydroquinone reached 83 %. The use of whole-cells of the wild type strain resulted in an alpha-arbutin concentration of 4 g/L and a molar conversion of 16 % only under the same conditions. The results suggested that E. coli displaying transglucosidase using truncated INPNC as an anchoring motif can be employed as a whole-cell biocatalyst in glucosylation. Recombinant E. coli displaying transglucosidase on the surface was used as whole-cell biocatalyst in hydroquinone glucosylation, and its enzymatic characteristics were also studied. The enzymatic activity of recombinant E. coli was seven to twelve-fold higher than that of X. campestris when using the same amount of cells. In the enzymatic characterization experiments, the optimal temperature was found to be 40℃. The optimum pH for the glucosylation of hydroquinone by E. coli displaying transglucosidase was 7.2. In the study of the effect of hydroquinone on the conversion of alpha-arbutin, it was found that the inhibitory effect of hydroquinone was profound at high concentrations of hydroquinone. In addition, conversion of hydroquinone to arbutin was inhibited slightly by high initial concentration of arbutin in the reaction mixture. Taken together, the results demonstrated that the enzyme was inhibited by both substrate and product. A fed-batch culture strategy for the high-cell density cultivation of recombinant E. coli cells anchoring surface-displayed transglucosidase for use as a whole-cell biocatalyst for alpha-arbutin synthesis was developed. Lactose was used as an inducer of the recombinant protein. In fed-batch cultures, dissolved oxygen was used as a feed indicator for glucose, thus accumulation of glucose and acetate that affected the cell growth and recombinant protein production was avoided. Fed-batch fermentation with lactose induction yielded a biomass of 18 g/L, and the cells possessed very high transglucosylation activity. In the synthesis of alpha-arbutin by hydroquinone glucosylation, the whole-cell biocatalysts showed a specific activity of 501 nkat/g cell and produced 21 g/L of arbutin, which corresponded to 76 % molar conversion. A sixfold increased productivity of whole cell biocatalysts was obtained in the fed-batch culture with lactose induction, as compared to batch culture induced by IPTG. We have successfully demonstrated the application of fed-batch culture strategy for the production of recombinant E. coli cells anchoring surface-displayed transglucosidase, for use as a biocatalyst in alpha-arbutin synthesis. Although the transglucosylating activity of recombinant cells using lactose as an inducer was slightly lower than that of the biocatalyst produced by IPTG induction, the use of fed-batch culture by lactose induction resulted in a higher productivity of whole cell biocatalysts. Therefore, fed-batch cultivation coupled with lactose induction offers an attractive strategy for the mass production of recombinant E. coli cells for use as whole-cell biocatalysts in biotransformations such as alpha-arbutin synthesis.
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Vanderveer, Tara Lynn. "The function, characterization of expression, localization and activity of a divergent ice nucleating protein from Pseudomonas borealis." Thesis, 2012. http://hdl.handle.net/1974/7200.
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An ice nucleating protein (INP) with 66% amino acid sequence identity to the better-known INP of Pseudomonas syringae has been described in an environmental isolate of P. borealis and designated InaPb. Despite the fact that INPs are classified as ice-binding proteins, InaPb showed little affinity for pre-formed ice and showed incorporation rates similar to Ina- strains. Additionally, it appeared to lack in the ability to shape ice or limit its growth. However, it was an effective ice nucleator. Using the coding sequence for InaPb and a green fluorescent protein tag (GFP), an InaPb-GFP fusion protein construct was inserted into a broad host expression vector in order to visualize the expression and localization of the protein in E. coli and an Ina- strain of P.syringae. The InaPb-GFP protein appears to localize at the poles of E. coli, but the nucleation temperature for these cells was only marginally above -9°C, which indicated poor nucleation activity. When expressed in Ina- P. syringae, the proteins showed clustering throughout the cell and an increased ability to nucleate ice following cold conditioning. The ability to nucleate ice was further increased by the removal of the GFP tag resulting in an average nucleation temperature more consistent with that seen in the native host P. borealis. Since inaPb transcript levels did not appear to change after cold conditioning, the clustering seen using fluorescence microscopy was likely the result of increased aggregation of protein in the membrane. Most INP-
producing bacteria are associated with plant disease, but experiments with P. borealis suggested that the Ina+ phenotype was not indicative of pathogenicity in this strain. It is hoped that my contribution to the functional characterization of this INP will lead to a better understanding of these special proteins and their importance to the handful of bacteria that exhibit this activity.Thesis (Master, Biology) -- Queen's University, 2012-05-15 09:55:52.506
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Huva, Emily. "Tetrahydrofuran Hydrate Inhibitors: Ice-Associating Bacteria and Proteins." Thesis, 2008. http://hdl.handle.net/1974/1728.
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Ice-associating proteins (IAPs) are proteins that interact directly with ice crystals, either by offering a site for nucleation, i.e. ice nucleating proteins (INPs), or by binding to nascent crystals to prevent addition of more water molecules, i.e. antifreeze proteins (AFPs). AFPs have been found to inhibit the formation of clathrate-hydrates, ice-like crystalline solids composed of water-encaged guest molecules. Study of AFP-hydrate interaction is leading to a greater understanding of AFP adsorption and of the mechanism behind the “memory effect” in hydrates, wherein previously frozen crystals reform more quickly after a brief melt. AFP is currently the only known memory inhibitor. Such a low-dosage hydrate inhibitor (LDHI) is of great interest to the oil and gas industry, as hydrate formation and reformation in the field is a huge problem. Bacterial AFPs, though largely uncharacterized, may be the best candidates for large-scale production of hydrate inhibitors, given the difficulties in obtaining AFP from other sources.
The popular kinetic inhibitors (KIs) polyvinylpyrrolidone (PVP) and polyvinylcaprolactam (PVCap) were used for points of comparison in experiments exploring the hydrate-inhibition activity of several ice-associating bacteria and proteins. The addition of the soil microbe, Chryseobacterium, increased the average lag-time to tetrahydrofuran (THF) hydrate formation by 14-fold, comparable to PVP or PVCap. Samples containing Pseudomonas putida, a bacterium having both ice-nucleation protein (INP) and AFP activity, had lag-times double that of the control. Solutions with P. putida and Chryseobacterium sometimes formed hydrate slurries of stunted crystal nuclei instead of solid crystals. No inhibition of memory or nucleation was noted in bacterial assays, however bacteria with INP activity was linked to unusually rapid memory reformation. Quartz crystal microbalance experiments with dissipation (QCM-D) showed that a tight adsorption to SiO2 and resistance to rinsing are correlated with a molecule’s inhibition of hydrate formation and reformation. These results support a heterogeneous nucleation model of the memory effect, and point to the affinity of AFP for heterogeneous nucleating particles as an important component of memory inhibition.Thesis (Master, Biology) -- Queen's University, 2008-05-30 15:20:38.749
Books on the topic "Ice nucleation protein"
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Clarke, Andrew. Freezing. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0006.
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Freezing is a widespread ecological challenge, affecting organisms in over half the terrestrial environment as well as both polar seas. With very few exceptions, if a cell freezes internally, it dies. Polar teleost fish in shallow waters avoid freezing by synthesising a range of protein or glycoprotein antifreezes. Terrestrial organisms are faced with a far greater thermal challenge, and exhibit a more complex array of responses. Unicellular organisms survive freezing temperatures by preventing ice nucleating within the cytosol, and tolerating the cellular dehydration and membrane disruption that follows from ice forming in the external environment. Multicellular organisms survive freezing temperatures by manipulating the composition of the extracellular body fluids. Terrestrial organisms may freeze at high subzero temperatures, often promoted by ice nucleating proteins, and small molecular mass cryoprotectants (often sugars and polyols) moderate the osmotic stress on cells. A range of chaperone proteins (dehydrins, LEA proteins) help maintain the integrity of membranes and macromolecules. Thermal hysteresis (antifreeze) proteins prevent damaging recrystallisation of ice. In some cases arthropods and higher plants prevent freezing in their extracellular fluids and survive by supercooling. Vitrification of extracellular water, or of the cell cytosol, may be a more widespread response to very cold temperatures than recognised to date.
Book chapters on the topic "Ice nucleation protein"
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Wolber, Paul K., and Gareth J. Warren. "Evolutionary Perspective on the Ice Nucleation Gene-Encoded Membrane Protein." In Brock/Springer Series in Contemporary Bioscience, 315–30. New York, NY: Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4612-3168-4_16.
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Duman, J. G., D. W. Wu, K. L. Yeung, and E. E. Wolf. "Hemolymph Proteins Involved in the Cold Tolerance of Terrestrial Arthropods: Antifreeze and Ice Nucleator Proteins." In Water and Life, 282–300. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76682-4_17.
Full textConference papers on the topic "Ice nucleation protein"
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Murakami, Daisuke, and Kenji Yasuoka. "Molecular Dynamics Simulation of Quasi-Two-Dimensional Water Network on Ice Nucleation Protein." In ASME/JSME 2011 8th Thermal Engineering Joint Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/ajtec2011-44609.
Full textAbstract:
An ice nucleation protein induces a phase transition from liquid water to ice in air. A specific hydrophilic surface of the protein may have an influence on the network of hydrogen bonds touching on the protein. However, microscopic characteristics of the ice nucleation protein and behavior of water molecules on it have not been clarified. So we carried out molecular dynamics simulations in various quasi-two-dimensional densities of water molecules on the ice nucleation protein. The percolation threshold of water clusters was confirmed. Comparing another hydrophilic protein, the threshold density in both cases had nearly the same value. But percolation probabilities and mean cluster sizes near the threshold were different between both cases. Those results implied that the threshold density was consistent with the conventional theory, but the forming of water clusters near the threshold was influenced by the hydrophilicity on the ice nucleation protein.