ArticleJournal of industrial microbiology & biotechnology2013
A low molecular mass cutinase of Thielavia terrestris efficiently hydrolyzes poly(esters).
Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 98 citations in OpenAlex.
- Lipases and Cutinases from Phytopathogenic and Saprobic Fungi in Plastic.Methods in molecular biology (Clifton, N.J.) · 2027Article
- The Absence of Sec72 Reshapes Yeast Cell Functions to Increase Protein Secretion.Research (Washington, D.C.) · 2026Article
- Biochemical Characterization and Polyester-Binding/Degrading Capability of Two Cutinases fromMicroorganisms · 2025Article
- Current Understanding on the Heterogenous Expression of Plastic Depolymerising Enzymes inBioengineering (Basel, Switzerland) · 2025Review
- Enzyme Benchmarking with Polyethylene Furanoate Soluble Scaffolds for Directed Evolution of PEFases.ACS omega · 2024Article
- Exploring biodegradable alternatives: microorganism-mediated plastic degradation and environmental policies for sustainable plastic management.Archives of microbiology · 2024Review
- Synthesis of Short-Chain Alkyl Butyrate through Esterification Reaction Using ImmobilizedJournal of microbiology and biotechnology · 2023Article
- An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation.International journal of molecular sciences · 2022Review
- A Review of the Fungi That Degrade Plastic.Journal of fungi (Basel, Switzerland) · 2022Review
- Fungal Enzymes Involved in Plastics Biodegradation.Microorganisms · 2022Review
- Recent Advances in Biological Recycling of Polyethylene Terephthalate (PET) Plastic Wastes.Bioengineering (Basel, Switzerland) · 2022Review
- Lessons From Insect Fungiculture: From Microbial Ecology to Plastics Degradation.Frontiers in microbiology · 2022Article
- A minireview on the bioremediative potential of microbial enzymes as solution to emerging microplastic pollution.Frontiers in microbiology · 2022Review
- Genomic and transcriptomic analysis of the thermophilic lignocellulose-degrading fungus Thielavia terrestris LPH172.Biotechnology for biofuels · 2021Article
- Enzymatic Remediation of Polyethylene Terephthalate (PET)-Based Polymers for Effective Management of Plastic Wastes: An Overview.Frontiers in bioengineering and biotechnology · 2020Review
- Engineering the flagellar type III secretion system: improving capacity for secretion of recombinant protein.Microbial cell factories · 2019Article
- Active Site Flexibility as a Hallmark for Efficient PET Degradation by I. sakaiensis PETase.Biophysical journal · 2018Article
- Screening of commercial enzymes for poly(ethylene terephthalate) (PET) hydrolysis and synergy studies on different substrate sources.Journal of industrial microbiology & biotechnology · 2017Article
- High-level expression and characterization of a novel cutinase fromBiotechnology for biofuels · 2017Article
- Influence of surface charge, binding site residues and glycosylation on Thielavia terrestris cutinase biochemical characteristics.Applied microbiology and biotechnology · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A low molecular mass cutinase (designated TtcutA) from Thielavia terrestris was purified and biochemically characterized. The thermophilic fungus T. terrestris CAU709 secreted a highly active cutinase (90.4 U ml(-1)) in fermentation broth containing wheat bran as the carbon source. The cutinase was purified 19-fold with a recovery yield of 4.8 %. The molecular mass of the purified TtcutA was determined as 25.3 and 22.8 kDa using SDS-PAGE and gel filtration, respectively. TtcutA displayed optimal activity at pH 4.0 and 50 °C. It was highly stable up to 65 °C and in the broad pH range 2.5-10.5. Extreme stability in high concentrations (80 %, v/v) of solvents such as methanol, ethanol, acetone, acetonitrile, isopropanol, and dimethyl sulfoxide was observed for the enzyme. The K (m) values for this enzyme towards p-nitrophenyl (pNP) acetate, pNP butyrate, and pNP caproate were 7.7, 1.0, and 0.52 mM, respectively. TtcutA was able to efficiently degrade various ester polymers, including cutin, polyethylene terephthalate (PET), polycaprolactone (PCL), and poly(butylene succinate) (PBS) at hydrolytic rates of 3 μmol h(-1) mg(-1) protein, 1.1 mg h(-1) mg(-1) protein, 203.6 mg h(-1) mg(-1) protein, and 56.4 mg h(-1) mg(-1) protein, respectively. Because of these unique biochemical properties, TtcutA of T. terrestris may be useful in various industrial applications in the future.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.