The Hydrophobins HFBI and HFBII from <i>Trichoderma r</i><i>eesei</i> Showing Efficient Interactions with Nonionic Surfactants in Aqueous Two-Phase Systems

Linder, Markus B.; Selber, Klaus; Nakari-Setälä, Tiina; Qiao, Mingqiang; Kula, Maria‐Regina; Penttilä, Merja

doi:10.1021/bm0001493

Cited by 133 publications

(122 citation statements)

References 37 publications

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“…Firstly, it has been shown that fusion of a foreign protein with a secreted native protein can enhance its production (e.g. Nyyssönen et al, 1993), and secondly, HFBI as a fusion partner can facilitate the purification of recombinant proteins in aqueous two-phase purification (Linder et al, 2001;Selber et al, 2001).…”

Section: Resultsmentioning

confidence: 99%

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

et al. 2004

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Previous studies on Melanocarpus albomyces laccase have shown that this enzyme is very interesting for both basic research purposes and industrial applications. In order to obtain a reliable and efficient source for this laccase, it was produced in the filamentous fungus Trichoderma reesei. Two approaches were used: production of a non-fused laccase and a hydrophobin-laccase fusion protein. Both proteins were expressed in T. reesei under the cbh1 promoter, and significantly higher activities were obtained with the non-fused laccase in shake-flask cultures (corresponding to about 230 mg l "1 ). Northern blot analyses showed rather similar mRNA levels from both expression constructs. Western analysis indicated intracellular accumulation and degradation of the hydrophobin-laccase fusion protein, showing that production of the fusion was limited at the post-transcriptional level. No induction of the unfolded protein response pathway by laccase production was detected in the transformants by Northern hybridization. The most promising transformant was grown in a fermenter in batch and fed-batch modes. The highest production level obtained in the fed-batch culture was 920 mg l "1 . The recombinant laccase was purified from the culture supernatant after cleaving the major contaminating protein, cellobiohydrolase I, by papain. The recombinant and wild-type laccases were compared with regard to substrate kinetics, molecular mass, pH optimum, thermostability, and processing of the N-and C-termini, and they showed very similar properties.

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Section: Resultsmentioning

confidence: 99%

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

et al. 2004

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“…[44][45][46] Fluorolink F10 (F10/A-ammonium salt, F10 in the text) was obtained from Solvay Specialty Polymers (Italy). The reagents (octadecylmercaptan, dodecane, ethylene glycol, diiodomethane) and solvents ( n -hexane, 2-propanol, and methanol) were purchased from Sigma-Aldrich and used without further purifi cation.…”

Section: Methodsmentioning

confidence: 99%

Hydrophobin as a Nanolayer Primer That Enables the Fluorinated Coating of Poorly Reactive Polymer Surfaces

Gazzera

Corti

Pirrie

et al. 2015

Adv Materials Inter

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thick fi lm to achieve signifi cant durability and, therefore, requires a relatively large amount of fl uoropolymer. Alternative approaches, such as chemical grafting of fl uoropolymers by radical methods through irradiation, [ 6−8 ] plasma, [ 9−12 ] or direct fl uorination with fl uorine gas, [ 1,2,13 ] require only moderate amounts of fl uorinated surface modifi ers but are much more aggressive and, in some cases, potentially hazardous.Other possibilities involve functionalization with fl uorinated molecules/ polymers consisting of specifi c chemical moieties that are able to bind either covalently or noncovalently to the polymer surface. [ 4,5,14,15 ] However, to achieve sufficiently stable bonding, this general strategy requires the presence of reactive hydrophilic sites, typically OH groups, which are not typically observed on the surfaces of apolar, hydrophobic polymers, such as polyolefi ns, and need to be introduced via oxidizing pretreatments that are usually either energy-intensive or not environmentally friendly. [ 16−19 ] Expanding on this strategy, we present an effi cient, rapid, and more environmentally friendly method to perform the fl uorocarbon coating of hydrophobic polymer surfaces. The method is based on the use of hydrophobins, i.e., amphiphilic surface-active proteins, as a nanosized primer layer that adheres to the hydrophobic polymer surface, making the surface hydrophilic and preparing it for the subsequent binding of a fl uoropolymer containing ionic moieties.Hydrophobins are a class of nontoxic, surface-active, and fi lm-forming proteins that are produced by fi lamentous A new and simple method is presented to fl uorinate the surfaces of poorly reactive hydrophobic polymers in a more environmentally friendly way using the protein hydrophobin (HFBII) as a nanosized primer layer. In particular, HFBII, via electrostatic interactions, enables the otherwise ineffi cient binding of a phosphate-terminated perfl uoropolyether onto polystyrene, polypropylene, and low-density polyethylene surfaces. The binding between HFBII and the perfl uoropolyether depends signifi cantly on the environmental pH, reaching the maximum stability at pH 4. Upon treatment, the polymeric surfaces mostly retain their hydrophobic character but also acquire remarkable oil repellency, which is not observed in the absence of the protein primer. The functionalization proceeds rapidly and spontaneously at room temperature in aqueous solutions without requiring energy-intensive procedures, such as plasma or irradiation treatments.

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“…It is a recombinant chimeric protein consisting of two CBDs from T. reesei, which preparation is described by Linder et al [26]. To the N terminus of this construct the hydrophobin protein HFBI also from T. reesei was fused in order to facilitate the protein purification [27]. The sequence of the HFBI tag is: SNGNGNVCPP GLFSNPQCCA TQVL-GLIGLD CKVPSQNVYD GTDFRNVCAK TGAQPLC-CVA PVAGQALLCQ TAVGA.…”

Section: Cbd Samplesmentioning

confidence: 99%

“…The protein was produced in T. reesei using the cbh1 promoter. The protein was purified from the culture supernatant using the HFBI tag by surfactant extraction as described in [27]. Briefly, 2% Berol 532 (Akzo-Nobel, Sweden) was added to the supernatant.…”

Section: Cbd Samplesmentioning

confidence: 99%

Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains

Nigmatullin

Lovitt

Wright

et al. 2004

Colloids and Surfaces B: Biointerfaces

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Colloidal probe microscopy has been used to study the interaction between model cellulose surfaces and the role of cellulose binding domain (CBD), peptides specifically binding to cellulose, in interfacial interaction of cellulose surfaces modified with CBDs.The interaction between pure cellulose surfaces in aqueous electrolyte solution is dominated by double layer repulsive forces with the range and magnitude of the net force dependent on electrolyte concentration. AFM imaging reveals agglomeration of CBD adsorbed on cellulose surface. Despite an increase in surface charge owing to CBD binding to cellulose surface, force profiles are less repulsive for interactions involving, at least, one modified surface. Such changes are attributed to irregularity of the topography of protein surface and non-uniform distribution of surface charges on the surface of modified cellulose.Binding double CBD hybrid protein to cellulose surfaces causes adhesive forces at retraction, whereas separation curves obtained with cellulose modified with single CBD show small adhesion only at high ionic strength. This is possibly caused by the formation of the cross-links between cellulose surfaces in the case of double CBD.

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The Hydrophobins HFBI and HFBII from Trichoderma reesei Showing Efficient Interactions with Nonionic Surfactants in Aqueous Two-Phase Systems

Cited by 133 publications

References 37 publications

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme

Hydrophobin as a Nanolayer Primer That Enables the Fluorinated Coating of Poorly Reactive Polymer Surfaces

Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains

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