2019
DOI: 10.1016/j.polymertesting.2019.105959
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Modification of polyacrylonitrile fabric for antibacterial application by tetracycline immobilization

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Cited by 9 publications
(6 citation statements)
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“…In addition, the degree of ionization of the functional groups present in the laccase active site can also change with the change in the pH of the microenvironment. As a direct result, the affinity between the enzyme and the substrate may increase or decrease as the active site's ionization degree may change and new ionic interactions may occur 79 . The secondary interactions developed between the support matrix and the enzyme can be favorable regarding the amplitude in the pH range of the immobilized enzyme 80 …”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In addition, the degree of ionization of the functional groups present in the laccase active site can also change with the change in the pH of the microenvironment. As a direct result, the affinity between the enzyme and the substrate may increase or decrease as the active site's ionization degree may change and new ionic interactions may occur 79 . The secondary interactions developed between the support matrix and the enzyme can be favorable regarding the amplitude in the pH range of the immobilized enzyme 80 …”
Section: Resultsmentioning
confidence: 99%
“…As a direct result, the affinity between the enzyme and the substrate may increase or decrease as the active site's ionization degree may change and new ionic interactions may occur. 79 The secondary interactions developed between the support matrix and the enzyme can be favorable regarding the amplitude in the pH range of the immobilized enzyme. 80 At pH 3, the improvement in enzyme performance after immobilization in PAN is clear, while for free laccase, the most relevant results occurred at pH 5.…”
Section: Stability Test Of Immobilized Laccase At Different Phsmentioning
confidence: 99%
“…The majority of the isolated nitrilases were composed of one polypeptide with a molecular weight of 3045 kDa, which under certain conditions would assemble to create the active holoenzyme [118]. The enzyme appears to exist most frequently as a big aggregate with 626 subunits, although increased levels of solvents which are organic in nature, temperature, pH, salt, or even the enzyme itself can cause subunit interaction and subsequently stimulation, whereas the majority of enzymes exhibit substrate-dependent activation [119]. The primary enzyme in the enzymatic process for converting nitriles to amides, which are then transformed by amidases to the appropriate acid, is nitrile hydratase (NHase).…”
Section: Nitrilases and Nitrile Hydratasesmentioning
confidence: 99%
“…Both enzymes are produced under inducible or constitutive conditions, depending on the nutrients utilized during microbial cultivation (Yamada and Kobayashi 1996 ; Gong et al 2012 ), being an advantage for future studies on PAN waste biodegradation. The direct conversion of PAN into PAA by the action of nitrilases was demonstrated by incubating the polymer with commercial enzymes and measuring ammonia release (Matamá et al 2007 ) and analyzing the modifications in nitrilase-treated PAN by ATR-FTIR spectra (Akkaya and Ozseker 2019 ). The nitrile hydratase/amidase system produced by R .…”
Section: Enzymatic Activities and Pathways Involved In Microbial Ap Dmentioning
confidence: 99%