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Journal articles on the topic 'Hydrophobic'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

Scholtmeijer, Karin, Meike I. Janssen, Bertus Gerssen, Marcel L. de Vocht, Babs M. van Leeuwen, Theo G. van Kooten, Han A. B. Wösten, and Joseph G. H. Wessels. "Surface Modifications Created by Using Engineered Hydrophobins." Applied and Environmental Microbiology 68, no. 3 (March 2002): 1367–73. http://dx.doi.org/10.1128/aem.68.3.1367-1373.2002.

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ABSTRACT Hydrophobins are small (ca. 100 amino acids) secreted fungal proteins that are characterized by the presence of eight conserved cysteine residues and by a typical hydropathy pattern. Class I hydrophobins self-assemble at hydrophilic-hydrophobic interfaces into highly insoluble amphipathic membranes, thereby changing the nature of surfaces. Hydrophobic surfaces become hydrophilic, while hydrophilic surfaces become hydrophobic. To see whether surface properties of assembled hydrophobins can be changed, 25 N-terminal residues of the mature SC3 hydrophobin were deleted (TrSC3). In addition, the cell-binding domain of fibronectin (RGD) was fused to the N terminus of mature SC3 (RGD-SC3) and TrSC3 (RGD-TrSC3). Self-assembly and surface activity were not affected by these modifications. However, physiochemical properties at the hydrophilic side of the assembled hydrophobin did change. This was demonstrated by a change in wettability and by enhanced growth of fibroblasts on Teflon-coated with RGD-SC3, TrSC3, or RGD-TrSC3 compared to bare Teflon or Teflon coated with SC3. Thus, engineered hydrophobins can be used to functionalize surfaces.

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2

Pennacchio, Anna, Paola Cicatiello, Eugenio Notomista, Paola Giardina, and Alessandra Piscitelli. "New clues into the self-assembly of Vmh2, a basidiomycota class I hydrophobin." Biological Chemistry 399, no. 8 (July 26, 2018): 895–901. http://dx.doi.org/10.1515/hsz-2018-0124.

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Abstract Hydrophobins are fungal proteins that can self-assemble into amphiphilic films at hydrophobic-hydrophilic interfaces. Class I hydrophobin aggregates resemble amyloid fibrils, sharing some features with them. Here, five site-directed mutants of Vmh2, a member of basidiomycota class I hydrophobins, were designed and characterized to elucidate the molecular determinants playing a key role in class I hydrophobin self-assembly. The mechanism of fibril formation proposed for Vmh2 foresees that the triggering event is the destabilization of a specific loop (L1), leading to the formation of a β-hairpin, which in turn generates the β-spine of the amyloid fibril.

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3

Teertstra, Wieke R., Heine J. Deelstra, Miroslav Vranes, Ralph Bohlmann, Regine Kahmann, Jörg Kämper, and Han A. B. Wösten. "Repellents have functionally replaced hydrophobins in mediating attachment to a hydrophobic surface and in formation of hydrophobic aerial hyphae in Ustilago maydis." Microbiology 152, no. 12 (December 1, 2006): 3607–12. http://dx.doi.org/10.1099/mic.0.29034-0.

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Ustilago maydis contains one repellent and two class I hydrophobin genes in its genome. The repellent gene rep1 has been described previously. It encodes 11 secreted repellent peptides that result from the cleavage of a precursor protein at KEX2 recognition sites. The hydrophobin gene hum2 encodes a typical class I hydrophobin of 117 aa, while hum3 encodes a hydrophobin that is preceded by 17 repeat sequences. These repeats are separated, like the repellent peptides, by KEX2 recognition sites. Gene hum2, but not hum3, was shown to be expressed in a cross of two compatible wild-type strains, suggesting a role of the former hydrophobin gene in aerial hyphae formation. Indeed, aerial hyphae formation was reduced in a Δhum2 cross. However, the reduction in aerial hyphae formation was much more dramatic in the Δrep1 cross. Moreover, colonies of the Δrep1 cross were completely wettable, while surface hydrophobicity was unaffected and only slightly reduced in the Δhum2 and the Δhum2Δhum3 cross, respectively. It was also shown that the repellents and not the hydrophobins are involved in attachment of hyphae to hydrophobic Teflon. Deleting either or both hydrophobin genes in the Δrep1 strains did not further affect aerial hyphae formation, surface hydrophobicity and attachment. From these data it is concluded that hydrophobins of U. maydis have been functionally replaced, at least partially, by repellents.

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4

Ahn, Sang-Oh, Ho-Dong Lim, Sung-Hwan You, Dae-Eun Cheong, and Geun-Joong Kim. "Soluble Expression and Efficient Purification of Recombinant Class I Hydrophobin DewA." International Journal of Molecular Sciences 22, no. 15 (July 22, 2021): 7843. http://dx.doi.org/10.3390/ijms22157843.

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Hydrophobins are small proteins (<20 kDa) with an amphipathic tertiary structure that are secreted by various filamentous fungi. Their amphipathic properties provide surfactant-like activity, leading to the formation of robust amphipathic layers at hydrophilic–hydrophobic interfaces, which make them useful for a wide variety of industrial fields spanning protein immobilization to surface functionalization. However, the industrial use of recombinant hydrophobins has been hampered due to low yield from inclusion bodies owing to the complicated process, including an auxiliary refolding step. Herein, we report the soluble expression of a recombinant class I hydrophobin DewA originating from Aspergillus nidulans, and its efficient purification from recombinant Escherichia coli. Soluble expression of the recombinant hydrophobin DewA was achieved by a tagging strategy using a systematically designed expression tag (ramp tag) that was fused to the N-terminus of DewA lacking the innate signal sequence. Highly expressed recombinant hydrophobin DewA in a soluble form was efficiently purified by a modified aqueous two-phase separation technique using isopropyl alcohol. Our approach for expression and purification of the recombinant hydrophobin DewA in E. coli shed light on the industrial production of hydrophobins from prokaryotic hosts.

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5

Carro, Shirley, Valeria J. Gonzalez-Coronel, Jorge Castillo-Tejas, Hortensia Maldonado-Textle, and Nancy Tepale. "Rheological Properties in Aqueous Solution for Hydrophobically Modified Polyacrylamides Prepared in Inverse Emulsion Polymerization." International Journal of Polymer Science 2017 (2017): 1–13. http://dx.doi.org/10.1155/2017/8236870.

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Inverse emulsion polymerization technique was employed to synthesize hydrophobically modified polyacrylamide polymers with hydrophobe contents near to feed composition. Three different structures were obtained: multisticker, telechelic, and combined. N-Dimethyl-acrylamide (DMAM), n-dodecylacrylamide (DAM), and n-hexadecylacrylamide (HDAM) were used as hydrophobic comonomers. The effect of the hydrophobe length of comonomer, the initial monomer, and surfactant concentrations on shear viscosity was studied. Results show that the molecular weight of copolymer increases with initial monomer concentration and by increasing emulsifier concentration it remained almost constant. Shear viscosity measurements results show that the length of the hydrophobic comonomer augments the hydrophobic interactions causing an increase in viscosity and that the polymer thickening ability is higher for combined polymers.

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6

Serva, Alessandra, Mathieu Salanne, Martina Havenith, and Simone Pezzotti. "Size dependence of hydrophobic hydration at electrified gold/water interfaces." Proceedings of the National Academy of Sciences 118, no. 15 (April 5, 2021): e2023867118. http://dx.doi.org/10.1073/pnas.2023867118.

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Hydrophobic hydration at metal/water interfaces actively contributes to the energetics of electrochemical reactions, e.g. CO2 and N2 reduction, where small hydrophobic molecules are involved. In this work, constant applied potential molecular dynamics is employed to study hydrophobic hydration at a gold/water interface. We propose an adaptation of the Lum–Chandler–Weeks (LCW) theory to describe the free energy of hydrophobic hydration at the interface as a function of solute size and applied voltage. Based on this model we are able to predict the free energy cost of cavity formation at the interface directly from the free energy cost in the bulk plus an interface-dependent correction term. The interfacial water network contributes significantly to the free energy, yielding a preference for outer-sphere adsorption at the gold surface for ideal hydrophobes. We predict an accumulation of small hydrophobic solutes of sizes comparable to CO or N2, while the free energy cost to hydrate larger hydrophobes, above 2.5-Å radius, is shown to be greater at the interface than in the bulk. Interestingly, the transition from the volume dominated to the surface dominated regimes predicted by the LCW theory in the bulk is also found to take place for hydrophobes at the Au/water interface but occurs at smaller cavity radii. By applying the adapted LCW theory to a simple model addition reaction, we illustrate some implications of our findings for electrochemical reactions.

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7

Ohtaki, Shinsaku, Hiroshi Maeda, Toru Takahashi, Youhei Yamagata, Fumihiko Hasegawa, Katsuya Gomi, Tasuku Nakajima, and Keietsu Abe. "Novel Hydrophobic Surface Binding Protein, HsbA, Produced by Aspergillus oryzae." Applied and Environmental Microbiology 72, no. 4 (April 2006): 2407–13. http://dx.doi.org/10.1128/aem.72.4.2407-2413.2006.

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ABSTRACT Hydrophobic surface binding protein A (HsbA) is a secreted protein (14.5 kDa) isolated from the culture broth of Aspergillus oryzae RIB40 grown in a medium containing polybutylene succinate-co-adipate (PBSA) as a sole carbon source. We purified HsbA from the culture broth and determined its N-terminal amino acid sequence. We found a DNA sequence encoding a protein whose N terminus matched that of purified HsbA in the A. ozyzae genomic sequence. We cloned the hsbA genomic DNA and cDNA from A. oryzae and constructed a recombinant A. oryzae strain highly expressing hsbA. Orthologues of HsbA were present in animal pathogenic and entomopathogenic fungi. Heterologously synthesized HsbA was purified and biochemically characterized. Although the HsbA amino acid sequence suggests that HsbA may be hydrophilic, HsbA adsorbed to hydrophobic PBSA surfaces in the presence of NaCl or CaCl2. When HsbA was adsorbed on the hydrophobic PBSA surfaces, it promoted PBSA degradation via the CutL1 polyesterase. CutL1 interacts directly with HsbA attached to the hydrophobic QCM electrode surface. These results suggest that when HsbA is adsorbed onto the PBSA surface, it recruits CutL1, and that when CutL1 is accumulated on the PBSA surface, it stimulates PBSA degradation. We previously reported that when the A. oryzae hydrophobin RolA is bound to PBSA surfaces, it too specifically recruits CutL1. Since HsbA is not a hydrophobin, A. oryzae may use several types of proteins to recruit lytic enzymes to the surface of hydrophobic solid materials and promote their degradation.

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8

Kazmierczak, Pam, Dae Hyuk Kim, Massimo Turina, and Neal K. Van Alfen. "A Hydrophobin of the Chestnut Blight Fungus, Cryphonectria parasitica, Is Required for Stromal Pustule Eruption." Eukaryotic Cell 4, no. 5 (May 2005): 931–36. http://dx.doi.org/10.1128/ec.4.5.931-936.2005.

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ABSTRACT Hydrophobins are abundant small hydrophobic proteins that are present on the surfaces of many filamentous fungi. The chestnut blight pathogen Cryphonectria parasitica was shown to produce a class II hydrophobin, cryparin. Cryparin is the most abundant protein produced by this fungus when grown in liquid culture. When the fungus is growing on chestnut trees, cryparin is found only in the fungal fruiting body walls. Deletion of the gene encoding cryparin resulted in a culture phenotype typical of hydrophobin deletion mutants of other fungi, i.e., easily wettable (nonhydrophobic) hyphae. When grown on the natural substrate of the fungus, however, cryparin-null mutation strains were unable to normally produce its fungal fruiting bodies. Although the stromal pustules showed normal development initially, they were unable to erupt through the bark of the tree. The hydrophobin cryparin thus plays an essential role in the fitness of this important plant pathogen by facilitating the eruption of the fungal fruiting bodies through the bark of its host tree.

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9

Lumsdon, Simon O., John Green, and Barry Stieglitz. "Adsorption of hydrophobin proteins at hydrophobic and hydrophilic interfaces." Colloids and Surfaces B: Biointerfaces 44, no. 4 (September 2005): 172–78. http://dx.doi.org/10.1016/j.colsurfb.2005.06.012.

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10

Ebdon, J. R., B. J. Hunt, D. M. Lucas, I. Soutar, L. Swanson, and A. R. Lane. "Luminescence studies of hydrophobically modified, water-soluble polymers. I. Fluorescence anisotropy and spectroscopic investigations of the conformational behaviour of copolymers of acrylic acid and styrene or methyl methacrylate." Canadian Journal of Chemistry 73, no. 11 (November 1, 1995): 1982–94. http://dx.doi.org/10.1139/v95-245.

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Fluorescence spectroscopy and anisotropy measurements have been used to study a series of styrene – acrylic acid, STY–AA, and methyl methacrylate – acrylic acid, MMA–AA, copolymers in dilute methanolic and aqueous solutions. Copolymerization of either STY or MMA with AA has little effect upon the rate of intramolecular segmental motion in methanol solutions. In aqueous media, intramolecular hydrophobic aggregation occurs and restricts the macromolecular dynamics to an extent dependent upon pH, nature of the comonomer, and copolymer composition. The hydrophobic domains formed in these copolymer systems can solubilize organic guests. In this respect, STY is a more powerful modifier of AA-based polymer behaviours than is MMA. In general, the hydrophobic modification increases the solubilization power of the resultant polymer. Furthermore, the copolymers retain their solubilization capacities to higher values of pH the more hydrophobic the comonomer and the greater its content in the copolymer. The interiors of the hydrophobic aggregates reduce the mobilities of occluded guests: the microviscosities of the domain interiors depend upon the nature of the hydrophobe, pH, and copolymer composition. Keywords: fluorescence, anisotropy, water-soluble polymers, acrylic acid, hydrophobic modification.

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11

Su, Ziyang, Yu Zhang, Weidong Liu, Ruijing Han, Xuezhi Zhao, Xiaohuo Shi, Xingyu Lu, Yan Zhang, and Yujun Feng. "A Quantitative Approach to Determine Hydrophobe Content of Associating Polyacrylamide Using a Fluorescent Probe." Molecules 28, no. 10 (May 17, 2023): 4152. http://dx.doi.org/10.3390/molecules28104152.

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Hydrophobically associating polymers have found widespread applications in many domains due to their unique rheological behavior, which is primarily dictated by the hydrophobe content. However, the low fraction of hydrophobic monomers in polymers makes this parameter’s precise and straightforward measurement difficult. Herein, a variety of hydrophobically associating polyacrylamides (HAPAM) with different alkyl chain lengths (L) and hydrophobic contents ([H]) were prepared by post-modification and accurately characterized by 1H NMR spectroscopy. The maximal fluorescence emission intensity (I) of 8-anilino-1-naphthalenesulfonic acid, which is sensitive to hydrophobic environments, was then detected in those polymer solutions and shown as a ratio to that in the polymer-free solution (I0). It was found that I/I0 for 0.5 wt% HAPAM can be scaled versus CH, which is a variate related to both L and [H], as I/I0 = 1.15 + 1.09 × 108CH3.42, which was also verified to be applicable for hydrophobic associating hydrolyzed polyacrylamide (HHAPAM). This relationship provides a handy method for determining the hydrophobic content of hydrophobically associating polymers, particularly for field applications.

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12

Peñas, María M., Sigridur A. Ásgeirsdóttir, Iñigo Lasa, Francisco A. Culiañez-Macià, Antonio G. Pisabarro, Joseph G. H. Wessels, and Lucía Ramírez. "Identification, Characterization, and In Situ Detection of a Fruit-Body-Specific Hydrophobin of Pleurotus ostreatus." Applied and Environmental Microbiology 64, no. 10 (October 1, 1998): 4028–34. http://dx.doi.org/10.1128/aem.64.10.4028-4034.1998.

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ABSTRACT Hydrophobins are small (length, about 100 ± 25 amino acids), cysteine-rich, hydrophobic proteins that are present in large amounts in fungal cell walls, where they form part of the outermost layer (rodlet layer); sometimes, they can also be secreted into the medium. Different hydrophobins are associated with different developmental stages of a fungus, and their biological functions include protection of the hyphae against desiccation and attack by either bacterial or fungal parasites, hyphal adherence, and the lowering of surface tension of the culture medium to permit aerial growth of the hyphae. We identified and isolated a hydrophobin (fruit body hydrophobin 1 [Fbh1]) present in fruit bodies but absent in both monokaryotic and dikaryotic mycelia of the edible mushroom Pleurotus ostreatus. In order to study the temporal and spatial expression of the fbh1 gene, we determined the N-terminal amino acid sequence of Fbh1. We also synthesized and cloned the double-stranded cDNA corresponding to the full-length mRNA of Fbh1 to use it as a probe in both Northern blot and in situ hybridization experiments. Fbh1 mRNA is detectable in specific parts of the fruit body, and it is absent in other developmental stages.

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13

McCabe, Patricia M., and Neal K. Van Alfen. "Secretion of Cryparin, a Fungal Hydrophobin." Applied and Environmental Microbiology 65, no. 12 (December 1, 1999): 5431–35. http://dx.doi.org/10.1128/aem.65.12.5431-5435.1999.

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ABSTRACT Cryparin is a cell-surface-associated hydrophobin of the filamentous ascomycete Cryphonectria parasitica. This protein contains a signal peptide that directs it to the vesicle-mediated secretory pathway. We detected a glycosylated form of cryparin in a secretory vesicle fraction, but secreted forms of this protein are not glycosylated. This glycosylation occurred in the proprotein region, which is cleaved during maturation by a Kex2-like serine protease, leaving a mature form of cryparin that could be isolated from both the cell wall and culture medium. Pulse-chase labeling experiments showed that cryparin was secreted through the cell wall, without being bound, into the culture medium. The secreted protein then binds to the cell walls ofC. parasitica, where it remains. Binding of cryparin to the cell wall occurred in submerged culture, presumably because of the lectin-like properties unique to this hydrophobin. Thus, the binding of this hydrophobin to the cell wall is different from that of other hydrophobins which are reported to require a hydrophobic-hydrophilic interface for assembly.

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14

Bromley, Keith M., Ryan J. Morris, Laura Hobley, Giovanni Brandani, Rachel M. C. Gillespie, Matthew McCluskey, Ulrich Zachariae, Davide Marenduzzo, Nicola R. Stanley-Wall, and Cait E. MacPhee. "Interfacial self-assembly of a bacterial hydrophobin." Proceedings of the National Academy of Sciences 112, no. 17 (April 13, 2015): 5419–24. http://dx.doi.org/10.1073/pnas.1419016112.

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The majority of bacteria in the natural environment live within the confines of a biofilm. The Gram-positive bacterium Bacillus subtilis forms biofilms that exhibit a characteristic wrinkled morphology and a highly hydrophobic surface. A critical component in generating these properties is the protein BslA, which forms a coat across the surface of the sessile community. We recently reported the structure of BslA, and noted the presence of a large surface-exposed hydrophobic patch. Such surface patches are also observed in the class of surface-active proteins known as hydrophobins, and are thought to mediate their interfacial activity. However, although functionally related to the hydrophobins, BslA shares no sequence nor structural similarity, and here we show that the mechanism of action is also distinct. Specifically, our results suggest that the amino acids making up the large, surface-exposed hydrophobic cap in the crystal structure are shielded in aqueous solution by adopting a random coil conformation, enabling the protein to be soluble and monomeric. At an interface, these cap residues refold, inserting the hydrophobic side chains into the air or oil phase and forming a three-stranded β-sheet. This form then self-assembles into a well-ordered 2D rectangular lattice that stabilizes the interface. By replacing a hydrophobic leucine in the center of the cap with a positively charged lysine, we changed the energetics of adsorption and disrupted the formation of the 2D lattice. This limited structural metamorphosis represents a previously unidentified environmentally responsive mechanism for interfacial stabilization by proteins.

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15

Tanaka, Takumi, Yuki Terauchi, Akira Yoshimi, and Keietsu Abe. "Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation." Microorganisms 10, no. 8 (July 25, 2022): 1498. http://dx.doi.org/10.3390/microorganisms10081498.

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Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of Aspergillus hydrophobins are comprehensively discussed on the basis of recent findings. Multiple Aspergillus hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some Aspergillus hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air–liquid interface, RolA of Aspergillus oryzae self-assembles via four stages, and its self-assembled films consist of two layers, a rodlet membrane facing air and rod-like structures facing liquid. The self-assembly depends mainly on hydrophobin conformation and solution pH. Cys4–Cys5 and Cys7–Cys8 loops, disulfide bonds, and conserved Cys residues of RodA-like hydrophobins are necessary for self-assembly at the interface and for adsorption to solid surfaces. AfRodA helps Aspergillus fumigatus to evade recognition by the host immune system. RodA-like hydrophobins recruit cutinases to promote the hydrolysis of aliphatic polyesters. This mechanism appears to be conserved in Aspergillus and other filamentous fungi, and may be beneficial for their growth. Aspergilli produce various small secreted proteins (SSPs) including hydrophobins, hydrophobic surface–binding proteins, and effector proteins. Aspergilli may use a wide variety of SSPs to decompose solid polymers.

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16

Wiggins, Philippa M. "Hydrophobic hydration, hydrophobic forces and protein folding." Physica A: Statistical Mechanics and its Applications 238, no. 1-4 (April 1997): 113–28. http://dx.doi.org/10.1016/s0378-4371(96)00431-1.

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17

Ishida, Naoyuki, Kohei Matsuo, Koreyoshi Imamura, and Vincent S. J. Craig. "Hydrophobic Attraction Measured between Asymmetric Hydrophobic Surfaces." Langmuir 34, no. 12 (February 28, 2018): 3588–96. http://dx.doi.org/10.1021/acs.langmuir.7b04246.

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18

Gallo, Mariana, Simone Luti, Fabio Baroni, Ivan Baccelli, Eduardo Maffud Cilli, Costanza Cicchi, Manuela Leri, Alberto Spisni, Thelma A. Pertinhez, and Luigia Pazzagli. "Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features." International Journal of Molecular Sciences 24, no. 3 (January 23, 2023): 2251. http://dx.doi.org/10.3390/ijms24032251.

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Cerato-ulmin (CU) is a 75-amino-acid-long protein that belongs to the hydrophobin family. It self-assembles at hydrophobic–hydrophilic interfaces, forming films that reverse the wettability properties of the bound surface: a capability that may confer selective advantages to the fungus in colonizing and infecting elm trees. Here, we show for the first time that CU can elicit a defense reaction (induction of phytoalexin synthesis and ROS production) in non-host plants (Arabidopsis) and exerts its eliciting capacity more efficiently when in its soluble monomeric form. We identified two hydrophobic clusters on the protein’s loops endowed with dynamical and physical properties compatible with the possibility of reversibly interconverting between a disordered conformation and a β-strand-rich conformation when interacting with hydrophilic or hydrophobic surfaces. We propose that the plasticity of those loops may be part of the molecular mechanism that governs the protein defense elicitation capability.

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19

Jeffs, Lloyd B., Ilungo J. Xavier, Russell E. Matai, and George G. Khachatourians. "Relationships between fungal spore morphologies and surface properties for entomopathogenic members of the general Beauveria, Metarhizium, Paecilomyces,Tolypocladium, and Verticillium." Canadian Journal of Microbiology 45, no. 11 (November 1, 1999): 936–48. http://dx.doi.org/10.1139/w99-097.

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The surface properties of aerial conidia (AC) from 24 strains of entomopathogenic fungi were studied and compared using the salt-mediated aggregation and sedimentation (SAS) assay, electron microscopy, FITC-labelled lectins, and spore dimensions. Spores with rugose surfaces were hydrophobic, whereas hydrophilic spores had smooth surfaces. Correlation analysis found no link between spore dimensions and either hydrophobicity or surface carbohydrates. However, there was a strong positive correlation between spore hydrophobicity and surface carbohydrates. The three spore types of Beauveria bassiana were all shown to possess discrete surface hydrophobicities, which were also strongly linked to surface carbohydrate profiles. Various chemical treatments had pronounced effects on spore surface properties, with sodium dodecyl sulfate (SDS) and formic acid (FA) reducing both lectin binding and surface hydrophobicity. When FA-protein extracts were separated and analysed using SDS-PAGE, only the hydrophobic spores had low molecular weight hydrophobin-like peptides that were unglycosylated and contained disulfide bonds. The strains with hydrophilic AC had much lower levels of FA-extractable protein per spore dry weight compared to their more hydrophobic counterparts. Moreover, extracts of the more hydrophobic spores tended to have greater protein:carbohydrate ratios.Key words: fungi, spores, hydrophobicity, lectins, morphology, microbial insecticides, protein.

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20

Dobrynin, Andrey V., and Michael Rubinstein. "Hydrophobic Polyelectrolytes." Macromolecules 32, no. 3 (February 1999): 915–22. http://dx.doi.org/10.1021/ma981412j.

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21

Strauss, Ulrich P., and Yu Chih Chiao. "Hydrophobic polyampholytes." Macromolecules 19, no. 2 (March 1986): 355–58. http://dx.doi.org/10.1021/ma00156a020.

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22

FIELD, ROBERT W., and VANESSA LOBO. "Hydrophobic Pervaporation." Annals of the New York Academy of Sciences 984, no. 1 (March 2003): 401–10. http://dx.doi.org/10.1111/j.1749-6632.2003.tb06015.x.

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23

Yaminsky, Vassili V., and Erwin A. Vogler. "Hydrophobic hydration." Current Opinion in Colloid & Interface Science 6, no. 4 (August 2001): 342–49. http://dx.doi.org/10.1016/s1359-0294(01)00104-2.

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24

Parazak, Dennis P., Charles W. Burkhardt, Kevin J. McCarthy, and Mark P. Stehlin. "Hydrophobic flocculation." Journal of Colloid and Interface Science 123, no. 1 (May 1988): 59–72. http://dx.doi.org/10.1016/0021-9797(88)90221-4.

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25

Gallagher, James. "Hydrophobic help." Nature Energy 3, no. 12 (December 2018): 1022. http://dx.doi.org/10.1038/s41560-018-0304-z.

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26

Lipkowski, J. "Hydrophobic hydration." Journal of Thermal Analysis and Calorimetry 83, no. 3 (March 2006): 525–31. http://dx.doi.org/10.1007/s10973-005-7391-3.

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27

Ohno, Nobumichi, and Shintaro Sugai. "Isotope effects on hydrophobic interaction in hydrophobic polyelectrolytes." Macromolecules 18, no. 6 (November 1985): 1287–91. http://dx.doi.org/10.1021/ma00148a042.

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28

Zhu, Liqun, Guofang Hao, Yuan Chen, and Yizhi Chen. "Investigation on hydrophobic films from a hydrophobic powder." Applied Surface Science 261 (November 2012): 863–67. http://dx.doi.org/10.1016/j.apsusc.2012.07.149.

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29

Ashbaugh, Henry S., and Michael E. Paulaitis. "Entropy of Hydrophobic Hydration: Extension to Hydrophobic Chains." Journal of Physical Chemistry 100, no. 5 (January 1996): 1900–1913. http://dx.doi.org/10.1021/jp952387b.

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30

von Vacano, Bernhard, Rui Xu, Sabine Hirth, Ines Herzenstiel, Markus Rückel, Thomas Subkowski, and Ulf Baus. "Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange." Analytical and Bioanalytical Chemistry 400, no. 7 (April 5, 2011): 2031–40. http://dx.doi.org/10.1007/s00216-011-4902-x.

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31

Nakari-Setälä, Tiina, Joana Azeredo, Mariana Henriques, Rosário Oliveira, José Teixeira, Markus Linder, and Merja Penttilä. "Expression of a Fungal Hydrophobin in the Saccharomyces cerevisiae Cell Wall: Effect on Cell Surface Properties and Immobilization." Applied and Environmental Microbiology 68, no. 7 (July 2002): 3385–91. http://dx.doi.org/10.1128/aem.68.7.3385-3391.2002.

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ABSTRACT The aim of this work was to modify the cell surface properties of Saccharomyces cerevisiae by expression of the HFBI hydrophobin of the filamentous fungus Trichoderma reesei on the yeast cell surface. The second aim was to study the immobilization capacity of the modified cells. Fusion to the Flo1p flocculin was used to target the HFBI moiety to the cell wall. Determination of cell surface characteristics with contact angle and zeta potential measurements indicated that HFBI-producing cells are more apolar and slightly less negatively charged than the parent cells. Adsorption of the yeast cells to different commercial supports was studied. A twofold increase in the binding affinity of the hydrophobin-producing yeast to hydrophobic silicone-based materials was observed, while no improvement in the interaction with hydrophilic carriers could be seen compared to that of the parent cells. Hydrophobic interactions between the yeast cells and the support are suggested to play a major role in attachment. Also, a slight increase in the initial adsorption rate of the hydrophobin yeast was observed. Furthermore, due to the engineered cell surface, hydrophobin-producing yeast cells were efficiently separated in an aqueous two-phase system by using a nonionic polyoxyethylene detergent, C12-18EO5.

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32

Chou, Chun-Tu, Shih-Chen Shi, and Chih-Kuang Chen. "Sandwich-Structured, Hydrophobic, Nanocellulose-Reinforced Polyvinyl Alcohol as an Alternative Straw Material." Polymers 13, no. 24 (December 18, 2021): 4447. http://dx.doi.org/10.3390/polym13244447.

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An environmentally friendly, hydrophobic polyvinyl alcohol (PVA) film was developed as an alternative to commercial straws for mitigating the issue of plastic waste. Nontoxic and biodegradable cellulose nanocrystals (CNCs) and nanofibers (CNFs) were used to prepare PVA nanocomposite films by blade coating and solution casting. Double-sided solution casting of polyethylene-glycol–poly(lactic acid) (PEG–PLA) + neat PLA hydrophobic films was performed, which was followed by heat treatment at different temperatures and durations to hydrophobize the PVA composite films. The hydrophobic characteristics of the prepared composite films and a commercial straw were compared. The PVA nanocomposite films exhibited enhanced water vapor barrier and thermal properties owing to the hydrogen bonds and van der Waals forces between the substrate and the fillers. In the sandwich-structured PVA-based hydrophobic composite films, the crystallinity of PLA was increased by adjusting the temperature and duration of heat treatment, which significantly improved their contact angle and water vapor barrier. Finally, the initial contact angle and contact duration (at the contact angle of 20°) increased by 35% and 40%, respectively, which was a significant increase in the service life of the biodegradable material-based straw.

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33

AKAHANE, Kenji, Yasuo NAGANO, and Hideaki UMEYAMA. "Hydrophobic effect on the protein-ligand interaction; Hydrophobic field-effect index and hydrophobic correlation index." CHEMICAL & PHARMACEUTICAL BULLETIN 37, no. 1 (1989): 86–92. http://dx.doi.org/10.1248/cpb.37.86.

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34

Wawrzyńczak, Agata, Hieronim Maciejewski, and Ryszard Fiedorow. "Hydrosilylation on Hydrophobic Material Supported Platinum Catalysts." Vestnik Volgogradskogo gosudarstvennogo universiteta. Serija 10. Innovatcionnaia deiatel’nost’, no. 1 (March 2015): 42–52. http://dx.doi.org/10.15688/jvolsu10.2015.1.6.

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35

Şengün, Yasemin, and Ayşe Erzan. "Hydrophobic chains near hydrophobic surfaces—simulations in three dimensions." Journal of Physics: Condensed Matter 17, no. 14 (March 25, 2005): S1183—S1194. http://dx.doi.org/10.1088/0953-8984/17/14/007.

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36

Igawa, Manabu, Toshiyuki Abe, and Hiroshi Okochi. "Pertraction of Hydrophobic Organic Solutes with a Hydrophobic Membrane." Chemistry Letters 27, no. 7 (July 1998): 597–98. http://dx.doi.org/10.1246/cl.1998.597.

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37

Önder, P., and A. Erzan. "Statistics of a hydrophobic chain near a hydrophobic boundary." European Physical Journal E 9, S1 (December 2002): 467–76. http://dx.doi.org/10.1140/epje/i2002-10105-2.

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38

Onofrio, Angelo, Giovanni Parisi, Giuseppe Punzi, Simona Todisco, Maria Antonietta Di Noia, Fabrizio Bossis, Antonio Turi, Anna De Grassi, and Ciro Leonardo Pierri. "Distance-dependent hydrophobic–hydrophobic contacts in protein folding simulations." Phys. Chem. Chem. Phys. 16, no. 35 (2014): 18907–17. http://dx.doi.org/10.1039/c4cp01131g.

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39

Wosten, Han A. B., Onno M. H. de Vries, and Joseph G. H. Wessels. "Interfacial Self-Assembly of a Fungal Hydrophobin into a Hydrophobic Rodlet Layer." Plant Cell 5, no. 11 (November 1993): 1567. http://dx.doi.org/10.2307/3869739.

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40

Takahashi, Toru, Hiroshi Maeda, Sachiyo Yoneda, Shinsaku Ohtaki, Yohei Yamagata, Fumihiko Hasegawa, Katsuya Gomi, Tasuku Nakajima, and Keietsu Abe. "The fungal hydrophobin RolA recruits polyesterase and laterally moves on hydrophobic surfaces." Molecular Microbiology 57, no. 6 (August 17, 2005): 1780–96. http://dx.doi.org/10.1111/j.1365-2958.2005.04803.x.

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41

Fan, Hao, Xiaoqin Wang, Jiang Zhu, George T. Robillard, and Alan E. Mark. "Molecular dynamics simulations of the hydrophobin SC3 at a hydrophobic/hydrophilic interface." Proteins: Structure, Function, and Bioinformatics 64, no. 4 (June 12, 2006): 863–73. http://dx.doi.org/10.1002/prot.20936.

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42

Lv, Yongli, Sheng Zhang, Yunshan Zhang, Hongyao Yin, and Yujun Feng. "Hydrophobically Associating Polyacrylamide “Water-in-Water” Emulsion Prepared by Aqueous Dispersion Polymerization: Synthesis, Characterization and Rheological Behavior." Molecules 28, no. 6 (March 16, 2023): 2698. http://dx.doi.org/10.3390/molecules28062698.

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The hydrophobically associating polyacrylamide (HAPAM) is an important kind of water-soluble polymer, which is widely used as a rheology modifier in many fields. However, HAPAM products prepared in a traditional method show disadvantages including poor water solubility and the need for hydrocarbon solvents and appropriate surfactants, which lead to environmental pollution and increased costs. To solve these problems, we reported a novel kind of HAPAM “water-in-water” (w/w) emulsion and its solution properties. In this work, a series of cationic hydrophobic monomers with different alkyl chain lengths were synthesized and characterized. Then, HAPAM w/w emulsions were prepared by the aqueous dispersion polymerization of acrylamide, 2-methylacryloylxyethyl trimethyl ammonium chloride and a hydrophobic monomer. All these emulsions can be stored more than 6 months, showing excellent stability. An optical microscopy observation showed that the particle morphology and the particle size of the HAPAM emulsion were more regular and bigger than the emulsion without the hydrophobic monomer. The solubility tests showed that such HAPAM w/w emulsions have excellent solubility, which took no more than 180 s to dilute and achieve a homogeneous and clear solution. The rheology measurements showed that the HAPAM association increases with a hydrophobe concentration or the length of hydrophobic alkyl chains, resulting in better shear and temperature resistances. The total reduced viscosity was 124.42 mPa·s for cw101, 69.81 mPa·s for cw6-1, 55.38 mPa·s for cw8-0.25, 48.95 mPa·s for cw12-0.25 and 28 mPa·s for cw16-0.25 when the temperature increased from 30 °C to 90 °C. The cw8-2.0 that contains a 2 mol% hydrophobe monomer has the lowest value at 19.12 mPa·s due to the best association. Based on the excellent stability, solubility and rheological properties, we believe that these HAPAM w/w emulsions could find widespread applications.

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43

Sedigh, Rozhina. "Ultra-Hydrophobic Water." STEM Fellowship Journal 3, no. 1 (February 1, 2017): 23–29. http://dx.doi.org/10.17975/sfj-2017-004.

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When a drop of a viscous fluid is deposited on a bath of the same fluid that is vibrating, it is shown that it coalesces with this substrate or lifts off when the vibration of the surface is larger than g, leading to a steady condition where a drop can be kept bouncing for any length of time, as shown in figure 1. The phenomena that will occur depends on various parameters, such as drop impact acceleration, liquid surface tension, density, dynamic viscosity, gravity, droplet radius and impact speed, bath vibration frequency and amplitude. The effect of different parameters will conclude to a set of conditions which results in a system, called “ultra-hydrophobic water” which plays important role in chemical micro fluidic applications.

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44

Adams, Daniel O. "Hydrophobic ear plugs." Journal of the Acoustical Society of America 100, no. 2 (1996): 692. http://dx.doi.org/10.1121/1.416224.

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45

Ostrovskaya, L. Yu, V. G. Ral’chenko, I. I. Vlasov, A. A. Khomich, and A. P. Bol’shakov. "Hydrophobic diamond films." Protection of Metals and Physical Chemistry of Surfaces 49, no. 3 (May 2013): 325–31. http://dx.doi.org/10.1134/s2070205113030118.

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46

Tondi, G., and A. Petutschnigg. "Hydrophobic tannin foams." International Wood Products Journal 6, no. 3 (May 19, 2015): 148–50. http://dx.doi.org/10.1179/2042645315y.0000000007.

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47

Knizek, Roman, Jakub Wiener, Oldrich Jirsak, Ludmila Fridrichova, and Vladimir Bajzik. "Hydrophobic Nanofiber Layers." Advanced Science Letters 19, no. 2 (February 1, 2013): 605–8. http://dx.doi.org/10.1166/asl.2013.4726.

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48

Huque, Entazul M. "The hydrophobic effect." Journal of Chemical Education 66, no. 7 (July 1989): 581. http://dx.doi.org/10.1021/ed066p581.

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49

Paulaitis, Michael E., Shekhar Garde, and Henry S. Ashbaugh. "The hydrophobic effect." Current Opinion in Colloid & Interface Science 1, no. 3 (June 1996): 376–83. http://dx.doi.org/10.1016/s1359-0294(96)80137-3.

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50

Murakami, Yukito, Yoshio Hisaeda, and Teruhisa Ohno. "Hydrophobic vitamin B12." Bioorganic Chemistry 18, no. 1 (March 1990): 49–62. http://dx.doi.org/10.1016/0045-2068(90)90015-w.

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