2012
DOI: 10.1016/j.enzmictec.2012.01.006
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Laccase- and chloroperoxidase-nanotube paint composites with bactericidal and sporicidal activity

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Cited by 37 publications
(40 citation statements)
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“…It has been proposed that lytic enzymes have evolved to target nonredundant defense features within the peptidoglycan cell wall, thus making it unlikely for the target microbes to develop efficient mechanisms of resistance to lytic enzyme activity (2,12). This approach, therefore, may be important for addressing the growing concern posed by antimicrobial resistance and could be very useful in future applications (51)(52)(53).…”
Section: Discussionmentioning
confidence: 99%
“…It has been proposed that lytic enzymes have evolved to target nonredundant defense features within the peptidoglycan cell wall, thus making it unlikely for the target microbes to develop efficient mechanisms of resistance to lytic enzyme activity (2,12). This approach, therefore, may be important for addressing the growing concern posed by antimicrobial resistance and could be very useful in future applications (51)(52)(53).…”
Section: Discussionmentioning
confidence: 99%
“…However, such coatings have shown limitations with regard to the photocatalyst leaching out [25], or the H 2 O 2 decontaminant not being strong enough to allow decontamination of more resilient pathogens such as spores [23,[26][27][28]. Recently, our group has shown that enzyme-carbon nanomaterial-based conjugates entrapped into polymer or paint-based coatings can generate potent decontamination agents such as hypochlorous or peracetic acids [29,30]. Using such coatings, decontamination was achieved upon addition of specific enzyme substrates, e.g.…”
Section: Introductionmentioning
confidence: 98%
“…for perhydrolase S54 V (AcT)-carbon nanotubes conjugates encapsulated into latex-based paints, peracetic acid was produced in the presence of propylene glycol diacetate and H 2 O 2 as substrates, yielding the efficient decontamination of both Escherichia coli (E. coli) and Bacillus cereus (B. cereus) [31]. Similarly, laccase-or chloroperoxidasecarbon nanotubes conjugates encapsulated into paints allowed decontamination of E. coli and Staphylococcus aureus, with laccase showing further decontamination capability against B. cereus and Bacillus anthracis, after the addition of the respective substrates for each enzyme (i.e., H 2 O 2 for chloroperoxidase and I − anions for laccase) [30]. In these studies the carbon nanotubes enhanced enzyme stability, while their high surface area to volume aspect ratios allowed for high enzyme loadings and thus retention of the enzyme-nanosupport conjugates into the coatings [31][32][33][34][35].…”
Section: Introductionmentioning
confidence: 99%
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“…Furthermore, the stability, under both storage and operational conditions, e.g., towards denaturation by heat or organic solvents, can be enhanced [7]. Currently, a range of supports have been reported for the immobilization of CPO, such as mesoporous supports [6,8,9], solgels [10,11], multi-walled carbon nanotubes [12,13] and other inorganic or organic solid supports [14,15]. The binding of an enzyme to a support (carrier) can be physical, ionic, or covalent in nature.…”
Section: Introductionmentioning
confidence: 99%