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Production of cutinase from Fusarium falciforme and its application for hydrophilicity improvement of polyethylene terephthalate fabric.

ABSTRACT: Among 23 isolates of cutinase-producing fungi from Thailand, one strain of Fusarium falciforme PBURU-T5 exhibited the greatest cutinase activity (3.36?±?0.12 U ml-1) against p-nitrophenyl butyrate. This strain was found to produce an inducible cutinase when cultivated in the liquid mineral medium containing cutin from papaya peel as the sole carbon source. By optimizing the production condition based on the central composite experimental design, the maximal cutinase activity up to 4.82?±?0.18 U ml-1 was attained under the condition: 0.4% (w/v) papaya cutin as the carbon source, 0.3% (w/v) peptone as the nitrogen source, incubation temperature at 30 °C for 4 days, and initial pH 7.0. The crude enzyme was optimally active at 35 °C and pH 9.0 which was suitable for textile industrial application. The treatment with the crude PBURU-T5 cutinase (100 U g-1 dry weight of fabric) could enhance the wetting time, water adsorption and moisture regain of polyethylene terephthalate fabric up to 1.9-, 1.2- and 1.3-fold, respectively, comparing with the conventional 1M NaOH treatment. The increment of these fabric properties by enzymatic treatment could facilitate the dyeing process and enhance the fabric softness. Thus, F. falciforme PBURU-T5 is the promising source of cutinase for the modification of the PET fabric surface.

SUBMITTER: Sooksai T

PROVIDER: S-EPMC6785599 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Production of cutinase from Fusarium falciforme and its application for hydrophilicity improvement of polyethylene terephthalate fabric.

Sooksai Taweeporn T Bankeeree Wichanee W Sangwatanaroj Usa U Lotrakul Pongtharin P Punnapayak Hunsa H Prasongsuk Sehanat S

3 Biotech 20191009 11

Among 23 isolates of cutinase-producing fungi from Thailand, one strain of Fusarium falciforme PBURU-T5 exhibited the greatest cutinase activity (3.36 ± 0.12 U ml-1) against p-nitrophenyl butyrate. This strain was found to produce an inducible cutinase when cultivated in the liquid mineral medium containing cutin from papaya peel as the sole carbon source. By optimizing the production condition based on the central composite experimental design, the maximal cutinase acti ...[more]

PMID: 31656727

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Project description:Cutinases have shown potential for hydrolysis of the recalcitrant synthetic polymer polyethylene terephthalate (PET). We have shown previously that the rate of this hydrolysis can be enhanced by the addition of hydrophobins, small fungal proteins that can alter the physicochemical properties of surfaces. Here we have investigated whether the PET-hydrolyzing activity of a bacterial cutinase from Thermobifida cellulosilytica (Thc_Cut1) would be further enhanced by fusion to one of three Trichoderma hydrophobins, i.e., the class II hydrophobins HFB4 and HFB7 and the pseudo-class I hydrophobin HFB9b. The fusion enzymes exhibited decreased kcat values on soluble substrates (p-nitrophenyl acetate and p-nitrophenyl butyrate) and strongly decreased the hydrophilicity of glass but caused only small changes in the hydrophobicity of PET. When the enzyme was fused to HFB4 or HFB7, the hydrolysis of PET was enhanced >16-fold over the level with the free enzyme, while a mixture of the enzyme and the hydrophobins led only to a 4-fold increase at most. Fusion with the non-class II hydrophobin HFB9b did not increase the rate of hydrolysis over that of the enzyme-hydrophobin mixture, but HFB9b performed best when PET was preincubated with the hydrophobins before enzyme treatment. The pattern of hydrolysis by the fusion enzymes differed from that of Thc_Cut1 as the concentration of the product mono(2-hydroxyethyl) terephthalate relative to that of the main product, terephthalic acid, increased. Small-angle X-ray scattering (SAXS) analysis revealed an increased scattering contrast of the fusion proteins over that of the free proteins, suggesting a change in conformation or enhanced protein aggregation. Our data show that the level of hydrolysis of PET by cutinase can be significantly increased by fusion to hydrophobins. The data further suggest that this likely involves binding of the hydrophobins to the cutinase and changes in the conformation of its active center.

Dataset Information

Production of cutinase from Fusarium falciforme and its application for hydrophilicity improvement of polyethylene terephthalate fabric.

Publications

Production of cutinase from <i>Fusarium falciforme</i> and its application for hydrophilicity improvement of polyethylene terephthalate fabric.

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