Screening of tropical fungi producing polyethylene terephthalate-hydrolyzing enzyme for fabric modification

Nimchua, Thidarat; Eveleigh, D. E.; Sangwatanaroj, Usa; Punnapayak, Hunsa

doi:10.1007/s10295-008-0356-3

Cited by 41 publications

(19 citation statements)

References 25 publications

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“…Cutinase is one of these enzymes, and cutinases from F. solani f. sp. pisi (6,10,26,36), F. oxysporum (25), and T. fusca (1,13,14,24,32) have been well studied regarding PET modification. However, the catalytic efficiencies of these enzymes are not sufficiently high to meet the requirements of the textile industry (10).…”

Section: Resultsmentioning

confidence: 99%

Isolation of a Novel Cutinase Homolog with Polyethylene Terephthalate-Degrading Activity from Leaf-Branch Compost by Using a Metagenomic Approach

Sulaiman

Yamato

Kanaya

et al. 2012

Appl Environ Microbiol

466

385

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The gene encoding a cutinase homolog, LC-cutinase, was cloned from a fosmid library of a leaf-branch compost metagenome by functional screening using tributyrin agar plates. LC-cutinase shows the highest amino acid sequence identity of 59.7% to Thermomonospora curvata lipase. It also shows the 57.4% identity to Thermobifida fusca cutinase. When LCcutinase without a putative signal peptide was secreted to the periplasm of Escherichia coli cells with the assistance of the pelB leader sequence, more than 50% of the recombinant protein, termed LC-cutinase*, was excreted into the extracellular medium. It was purified and characterized. LC-cutinase* hydrolyzed various fatty acid monoesters with acyl chain lengths of 2 to 18, with a preference for short-chain substrates (C 4 substrate at most) most optimally at pH 8.5 and 50°C, but could not hydrolyze olive oil. It lost activity with half-lives of 40 min at 70°C and 7 min at 80°C. LC-cutinase* had an ability to degrade poly(-caprolactone) and polyethylene terephthalate (PET). The specific PET-degrading activity of LC-cutinase* was determined to be 12 mg/h/mg of enzyme (2.7 mg/h/kat of pNP-butyrate-degrading activity) at pH 8.0 and 50°C. This activity is higher than those of the bacterial and fungal cutinases reported thus far, suggesting that LC-cutinase* not only serves as a good model for understanding the molecular mechanism of PET-degrading enzyme but also is potentially applicable for surface modification and degradation of PET. C utinase (EC 3.1.1.74) is a lipolytic/esterolytic enzyme that hydrolyzes not only cutin, which is a major component of plant cuticle (38), but also water-soluble esters and insoluble triglycerides (12). It hydrolyzes these substrates to carboxylic acids and alcohols through the formation of an acyl enzyme intermediate, in which the active-site serine residue is acylated by the substrate. This serine residue is located within a GXSXG sequence motif and forms a catalytic triad with His and Asp. Cutinase has been found in both fungi and bacteria. The crystal structures of two fungal cutinases from Fusarium solani f. sp. pisi (22) and Glomerella cingulata (27) have been determined. According to these structures, cutinase shares a common ␣/␤ hydrolase fold with lipase and esterase (28). However, cutinase, like esterase, does not have a lid structure, which is responsible for interfacial activation of lipase (8). Therefore, cutinase does not show interfacial activation like esterase (14). Cutinase has recently received much attention because of its potential application for surface modification and degradation of aliphatic and aromatic polyesters (16), especially polyethylene terephthalate (PET), which is a synthetic aromatic polyester composed of terephthalic acid (TPA) and ethylene glycol (10,16,36,39). However, the number of cutinases, which have been studied regarding PET modification, is still limited, and this limitation may result in the delay of the research toward the practical use of cutinases. Therefore, isolation of a novel cutinase...

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Section: Resultsmentioning

confidence: 99%

Isolation of a Novel Cutinase Homolog with Polyethylene Terephthalate-Degrading Activity from Leaf-Branch Compost by Using a Metagenomic Approach

Sulaiman

Yamato

Kanaya

et al. 2012

Appl Environ Microbiol

466

385

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“…The intent of our study was to isolate and describe a microorganism that can degrade and assimilate poly(ethylene terephthalate) (PET) (2). Therefore, we only cited the pioneering works that report specific microorganisms able to grow on PET (3,4). In a previous study, Sharon and Sharon (5) confirmed microbial PET degradation by semiisolated microorganisms, where the involvement of Nocardia species was implied by microscopic observation.…”

mentioning

confidence: 99%

Response to Comment on “A bacterium that degrades and assimilates poly(ethylene terephthalate)”

Yoshida

Hiraga

Takehana³

et al. 2016

Science

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Yang et al. suggest that the use of low-crystallinity poly(ethylene terephthalate) (PET) exaggerates our results. However, the primary focus of our study was identifying an organism capable of the biological degradation and assimilation of PET, regardless of its crystallinity. We provide additional PET depolymerization data that further support several other lines of data showing PET assimilation by growing cells of Ideonella sakaiensis. W e appreciate the Comment by Yang et al.(1) and are grateful for this opportunity to explain the context of how our work builds on previous studies. The intent of our study was to isolate and describe a microorganism that can degrade and assimilate poly(ethylene terephthalate) (PET) (2). Therefore, we only cited the pioneering works that report specific microorganisms able to grow on PET (3, 4). In a previous study, Sharon and Sharon (5) confirmed microbial PET degradation by semiisolated microorganisms, where the involvement of Nocardia species was implied by microscopic observation. However, the contribution of other microorganisms was not ruled out, nor was the possibility that the PET was degraded by the resting cells harboring PET-hydrolyzable enzymes. We identified the PET hydrolase (PETase) gene based on amino acid sequence identity with a known hydrolase from Thermobifida fusca (TfH) that exhibited PET-hydrolyzing activity (6), similar to other PET-hydrolyzing enzymes (7-10). We further referred cutinase from Humicola insolens (HiC) (11) and seven other enzymes in the supplementary materials [table S2 in (2)]. The functions of these enzymes, particularly TfH, LCC (9), and FsC (10), greatly contributed to the understanding of PETase enzymology.With the intention of isolating a specific microorganism that can use PET for growth, even if the PET is mostly in the amorphous form, the extent of crystallinity is of secondary importance. We described the motivation for using low-crystallinity (1.9%) PET and the observation that the structure of crystallized PET hampered the enzymatic hydrolysis of its ester linkages (8, 12) in our Report.Based on the proton nuclear magnetic resonance and gel permeation chromatography profiles of the degraded PET film, we concluded that the degradation by the consortium termed "no. 46" proceeded from the PET surface (2). To support this inference, we analyzed the surface of the PET film using x-ray photoelectron spectroscopy (XPS). The XPS spectrum for degraded PET film by no. 46 showed that a new peak appeared at 0.6 eV higher in binding energy than that observed for the O 1s peak of C-O-C linkage (532.5 eV), indicating the formation of the C-O-H linkage by hydrolysis of the ester linkage, which should either be of hydroxyl or carboxyl groups. To accurately determine the surface functional groups, each group was labeled with heptafluorobutyryl chloride (for -OH) and 1,1-carbonyldiimidazole (for -COOH) (13) and analyzed by XPS. Consequently, the peaks of F 1S (687.5 eV) and N 1S (398.5 eV) after degradation dramatically increased (Fig. 1A). The ...

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“…Nimchua et al reported that the agar plate assay for detecting the PET-hydrolysing enzyme of Fusarium spp. showed no correlation between the quantity of enzyme produced and the clearing zone development 15 . All four fungi decolourized wastewater No.…”

Section: Fungal Isolatementioning

confidence: 91%

Untitled

Prasongsuk¹,

Lotrakul²,

Imai³

et al. 2009

ScienceAsia

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Twenty isolates of white rot fungi were collected from several provinces in Thailand. Eight isolates could be cultured to test for thermotolerance and to screen for the presence of ligninolytic enzymes using Phanerochaete chrysosporium as a reference. Of the eight isolates, only three species Daedaleopsis sp., Schizophyllum commune PT, and S. commune SL were able to grow above 40°C. All three species exhibited 2,2 -azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS)-oxidizing activity on ABTS agar plates. Only P. chrysosporium could oxidize manganese on MnCl 2 agar plates. Both P. chrysosporium and Daedaleopsis sp. were able to decolourize wastewater on wastewater agar plates. All fungal cell suspensions tested decolourized wastewater No. 1 (pH 8.07, chemical oxygen demand (COD) 4347 mg/l) from the pulping process and wastewater No. 2 (pH 6.94, COD 4000 mg/l) from the pulping process combined with that from the paper recycling process. Daedaleopsis sp. and P. chrysosporium exhibited the highest ability to decolourize wastewater No. 1 (52%) and No. 2 (86%), respectively. Laccase activities were detected in the decolourized effluents and all fungi tested reduced the COD by 59-71% (No. 1) and 66-83% (No. 2).

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Screening of tropical fungi producing polyethylene terephthalate-hydrolyzing enzyme for fabric modification

Cited by 41 publications

References 25 publications

Isolation of a Novel Cutinase Homolog with Polyethylene Terephthalate-Degrading Activity from Leaf-Branch Compost by Using a Metagenomic Approach

Isolation of a Novel Cutinase Homolog with Polyethylene Terephthalate-Degrading Activity from Leaf-Branch Compost by Using a Metagenomic Approach

Response to Comment on “A bacterium that degrades and assimilates poly(ethylene terephthalate)”

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