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Microbial Mediated Biodegradation of Plastic Waste
Published in Amitava Rakshit, Manoj Parihar, Binoy Sarkar, Harikesh B. Singh, Leonardo Fernandes Fraceto, Bioremediation Science From Theory to Practice, 2021
Rajendra Prasad Meena, Sourav Ghosh, Surendra Singh Jatav, Manoj Kumar Chitara, Dinesh Jinger, Kamini Gautam, Hanuman Ram, Hanuman Singh Jatav, Kiran Rana, Surajyoti Pradhan, Manoj Parihar
Cutinases are involved in (catalyze) hydrolysis of cutin which are aliphatic polyesters and are found in plant cuticle structure. Under the super family of a/0 hydrolases, this category of polyester hydrolases acts upon several polyester plastics (Wei and Zimmermann 2017 a, b). Depending on their homology, origin, and structure, plastic-degrading cutinases can be divided into fungal and bacterial. Cutinases from fungal origin such as Therm omycesinsolens, Fusarium and Humicola are useful and show excellent activity in the hydrolysis and surface alterations of polyethylene terephthalate (PET) films and fibers (Zimmermann and Billig 2010), due to their remarkable activity and thermal stability at 70°C near the glass transition temperature of PET (Ronkvist et al. 2009). Bacterial cutinases capable of hydrolyzing PET have been segregated from various Thermobifida species (Then et al. 2015), Thermomonosporacurvata (Wei et al. 2014), Saccharomonosporaviridis (Kawai et al. 2014), Ideonellasakaiensis (Yoshida et al. 2016), as well as the metagenome isolated from plant compost (Sulaiman et al. 2012). The bacterium, Ideonellasakaiensis 201-F6, exhibits rare capability to thrive on PET as a major carbon and energy source and secretes PETase (PET-digesting enzyme) leading to its biodegradation (Yoshida et al. 2016).
Production, purification and application of Cutinase in enzymatic scouring of cotton fabric isolated from Acinetobacter baumannii AU10
Published in Preparative Biochemistry & Biotechnology, 2021
P. Gururaj, S. Khushbu, B. Monisha, N. Selvakumar, M. Chakravarthy, P. Gautam, G. Nandhini Devi
Cutinase has immense potential as industrial enzymes in other industries such as Food, Dairy, Detergents, Pharmaceutical, Bio-diesel, Agriculture, Fine Chemicals, Bioremediation, Biodegradation and particularly in the Textile Industry.[4] Cutinase (EC 3.1.1.74) is an enzyme that catalyzes the hydrolysis of ester bonds in cutin.[4–6] It is isolated from fungi,[6–9] bacteria[10–14] and plants.[15] The cultivation, maintenance and isolation of enzymes from plants are more complicated than microbial enzymes. Microbial enzymes are attractive because of the cost of production, maintenance and easy handling procedures.[16,17] This Microbial production of cutinase requires cutin as a substrate.
Analysis of polysaccharide hydrolases secreted by Aspergillus flavipes FP-500 on corn cobs and wheat bran as complex carbon sources
Published in Preparative Biochemistry & Biotechnology, 2020
Lizzete Ruth Torres-Barajas, María Teresa Alvarez-Zúñiga, Guillermo Mendoza-Hernández, Guillermo Aguilar-Osorio
From a total of proteins, 16% and 11% were classified as esterases produced in CC and WB, respectively. In this category were placed lipases and esterases (Figure 3a,b). Likewise, were considered the cutinases because although they are considered serin esterases, they are also hydrolases. On both substrates, a cutinase was produced. They were initially discovered because they are secreted by fungi to hydrolyze the ester bonds of the plant polymer cutin. Cutinases are able to hydrolyze a greater variety of substrates, including low-molecular-weight soluble esters, short- and long-chain triacylglycerols, and are also capable of catalyzing esterification and transesterification.[61] Also, it may have a function in nutrient uptake of an accessible carbon source, rather than as pathogenicity or virulence factor.[11]