Phytopathogenic fungi penetrate plants by breaking down the cuticular barrier with cutinase. Cutinases are extracellular hydrolytic enzymes that degrade cutin, a polyester composed of hydroxy and epoxy fatty acids. Until now, cutinase has been recognized by its ability to release labeled cutin monomers or by a non-specific esterase assay based on the hydrolysis of p-nitrophenyl esters of short fatty acids. In this work, an insoluble p-nitrophenyl derivative was synthesized and purified, and its structure was determined to be 4-nitrophenyl (16-methyl sulfone ester) hexadecanoate (pNMSEH) by nuclear magnetic resonance (H+ NMR) analysis. pNMSEH was tested as a new cutinase substrate with Pseudomonas mandocino cutinase and porcine liver esterase. While a linear release over time of p-nitrophenol (pNP) was recorded in the presence of cutinase, no response was obtained with the esterase. The calculated kinetic parameters of pNMSEH hydrolysis by cutinase revealed a high specificity (Km=1.8mM), albeit a low catalytic rate (Vmax=10.5 micromol min(-l)l(-1)). This new synthetic substrate may be helpful for detecting and assaying cutinase activity in mixed solutions, such as crude fungal extracellular extracts.
School of Biotechnology and Key Laboratory of Industrial Biotechnology Ministry of Education, China; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi 214122 China. Electronic address:
The substantial accumulation of polyethylene terephthalate (PET) plastic waste in the environment has exacerbated the issue of plastic pollution. The biodegradation of PET plastics using biological enzymes has garnered considerable attention due to its efficiency and environmentally friendly nature. Nevertheless, the low binding affinity of PET plastics presents a significant limitation to the application of biocatalysts in their degradation.
Biodegradation, particularly via enzymatic degradation, has emerged as an efficient and eco-friendly solution for Poly (ethylene terephthalate) (PET) pollution. The production of PET hydrolases plays a role in the large-scale enzymatic degradation. However, an effective variant, 4Mz, derived from Thermobifida fusca cutinase (Tfu_0883), was previously associated with a significant reduction in yield when compared to the wild-type enzyme.
Key Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture and Rural Affairs, College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China. Electronic address:
Biodegradation of polyurethane (PU) plastics is a lower cost and more environmentally friendly approach to the regeneration of waste plastics than the landfill or incineration alternatives. Currently, however, the lack of efficient degradation strains and their enzymes is restricting the development of viable large-scale waste PU regeneration. In this study, a wild strain (LTX1) is isolated from a coastal mudflat, and then a mutant strain (MLTX1) with higher degradation efficiency is obtained by UV mutagenesis.
Polyethylene terephthalate (PET) pollution is an emerging environmental hazard because of its recalcitrance to degradation. This study proposes an mutagenesis of LipKV1 from for improved lipase-PET interaction, using the PET-degrading cutinase (TfCut2) as the structural benchmark. Results revealed that lid deletion on LipKV1 (LipKV1_LE) facilitated the entry of PET into the active site.
Polyethylene (PE), widely utilized in everyday life, is notorious for its protracted degradation period, extending over decades, presenting an environmental hazard. Recently, there has been growing interest in utilizing microorganisms to aid in PE decomposition. Molecular docking and molecular dynamics simulations are valuable tools for understanding specific mechanisms and conducting initial screenings to support experimental research in this context.
