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RISS 인기검색어
- 검색키워드
- 저자 : Avinash A. Kadam (검색결과 6 건)
- 무료
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Kadam, Avinash A.,Jang, Jiseon,Lee, Dae Sung American Chemical Society 2017 ACS APPLIED MATERIALS & INTERFACES Vol.9 No.18
<P>Halloysite nanotubes (HNTs) were tuned with supermagnetic Fe3O4 (M-HNTs) and functionalized with beta-aminopropyltriethoxysilane (APTES) (A-M-HNTs). Gluteraldehyde (GTA) was linked to A-M-HNTs (A-M-HNTs-GTA) and explored for covalent laccase immobilization. The structural characterization of M-HNTs, A-M-HNTs, and A-M-HNTs-GTA-immobilized laccase (A-M-HNTs-GTA-Lac) was determined by X-ray photoelectron spectroscopy, field-emission high resolution transmission electron microscopy, a magnetic property measurement system, and thermogavimetric analyses. A-MHNTs-GTA-Lac gave 90.20% activity recovery and a loading capability of 84.26 mg/g, with highly improved temperature and storage stabilities. Repeated usage of A-M-HNTs-GTA-Lac revealed a remarkably consistent relative activity of 80.49% until the ninth cycle. The A-M-HNTs-GTA-Lac gave consistent redox-mediated sulfamethoxazole (SMX) degradation up to the eighth cycle. In the presence of guaiacol, A-M-HNTs-GTA-Lac gave elevated SMX degradation compared with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) and syrinialdehyde. Therefore, the A-M-HNTs can serve as supermagnetic aminofunctionalized nanoreactors for biomacromolecule immobilization. The obtained A-M-HNTs-GTA-Lac is an environmentally friendly biocatalyst for effective degradation of micropollutants, such as SMX, and can be easily retrieved from an aqueous solution by a magnet after decontamination of pollutants in water and wastewater.</P>
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Chitosan-functionalized supermagnetic halloysite nanotubes for covalent laccase immobilization
Kadam, Avinash A.,Jang, Jiseon,Jee, Seung Cheol,Sung, Jung-Suk,Lee, Dae Sung Elsevier 2018 Carbohydrate polymers Vol.194 No.-
<P><B>Abstract</B></P> <P>Halloysite nanotubes (HNTs) were modified with supermagnetic Fe<SUB>3</SUB>O<SUB>4</SUB> (M-HNTs) and functionalized with chitosan (CTA) (termed as M-HNTs–CTA). Furthermore, M-HNTs–CTA were cross-linked using glutaraldehyde and applied for covalent laccase immobilization (M-HNTs–CTA–<I>Lac</I>). Facile-synthesized modified HNTs were structurally characterized by scanning electron microscopy, high resolution transmission electron microscopy, X-ray photoelectron spectroscopy, and thermogravimetric analyses. M-HNTs–CTA–<I>Lac</I> exhibited 92.74 mg/g of laccase immobilization capacity and 92% of activity recovery. Biochemical properties of M-HNTs–CTA–<I>Lac</I> exhibited higher pH and temperature stabilities, with exceptional reusability capabilities until the 11<SUP>th</SUP> cycle. Moreover, M-HNTs–CTA–<I>Lac</I> exhibited 87% of 2,2′-azinobis (3-ethylbenzthiazoline-6-sulphonic acid) (ABTS)-mediated Direct Red 80 (DR80) decolorization. By the 11<SUP>th</SUP> cycle, M-HNTs–CTA–<I>Lac</I> exhibited 33% DR80 decolorization. Therefore, M-HNTs–CTA can function as CTA-modified supermagnetic nonreactors for immobilization of biomacromolecules. The investigated M-HNTs–CTA–<I>Lac</I> are thus biocompatible and environment-friendly biocatalysts for degradation of textile waste, such as DR80, and can be rapidly retrieved from aqueous solution by a magnet after decontamination of environmental pollutants.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Chitosan (CTA)-functionalized supermagnetic HNTs (M-HNTs) were synthesized. </LI> <LI> Laccase (<I>Lac</I>) was covalently immobilized on M-HNTs–CTA. </LI> <LI> M-HNTs–CTA–<I>Lac</I> exhibited better biocatalysis than free laccase. </LI> <LI> M-HNTs–CTA–<I>Lac</I> exhibited excellent degradation of Direct Red 80 (DR80). </LI> <LI> Repeated cycles of DR80 degradation confirmed sustainable and greener biocatalysis. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
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Amar A. Telke,Avinash A. Kadam,Sujit S. Jagtap,Jyoti P. Jadhav,Sanjay P. Govindwar 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.4
In our study, we produced intracellular blue laccase by growing the filamentous fungus Aspergillus ochraceus NCIM-1146 in potato dextrose broth. The enzyme was then purified 22-fold to a specific activity of 4.81 U/mg using anion-exchange and size exclusion chromatography. The molecular weight of purified laccase was estimated as 68 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme showed maximum substrate specificity toward 2,2'-Azinobis, 3-ethylbenzothiazoline-6-sulfonic acid than any other substrate. The optimum pH and temperature for laccase activity were 4.0 and 60ºC, respectively. The purified enzyme was stable up to 50ºC, and high laccase activity was maintained at pH 5.0 ~ 7.0. Laccase activity was strongly inhibited by sodium azide, EDTA, dithiothreitol, and L-cysteine. Purified laccase decolorized various textile dyes within 4 h in the absence of redox mediators. HPLC and FTIR analysis confirmed degradation of methyl orange. The metabolite formed after decolorization of methyl orange was characterized as p-N,N'-dimethylamine phenyldiazine using GCMS.
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Kim, Min,Jee, Seung Cheol,Sung, Jung-Suk,Kadam, Avinash A. Elsevier 2018 INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES Vol.118 No.1
<P><B>Abstract</B></P> <P>Owing to the ubiquitous availability and simple biocatalysis, the anti-proliferative laccase holds enormous opportunities for anti-cancer applications. However, accessing efficient and specific (super-magnetically targetable) new delivery system for anti-proliferative laccase is vital step towards laccase based anti-cancer approach. Therefore, in this investigation, super-magnetized (Fe<SUB>3</SUB>O<SUB>4</SUB>) and chitosan (CS) functionalized halloysite nanotubes (HNTs) (termed as Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS) was facile synthesized. Further, laccase from <I>Trametes versicolor</I> was immobilized on Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS (termed as Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS-<I>Lac</I>). Then free laccase and Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS-<I>Lac</I> were evaluated for anti-proliferative properties against cancer cell lines of liver (HepG2), lung (H460), cervix (Hela) and stomach (AGS). Laccase and Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS-<I>Lac</I> gave significant cytotoxicity against all studied cancer cell lines. Moreover, the apoptosis analysis and FE-SEM morphology observations of cells support the anti-proliferative potential of laccase immobilized on Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS. Therefore, investigated Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS-<I>Lac</I> is natural and super-magnetic nano-biocatalyst, having the significant anti-proliferative potential and furthermore, Fe<SUB>3</SUB>O<SUB>4</SUB>-HNTs-CS can be used as efficient and specific delivery system for other anti-cancer enzymes.</P> <P><B>Highlights</B></P> <P> <UL> <LI> <I>Trametes versicolor</I> laccase gave significant anti-proliferative properties. </LI> <LI> Laccase was immobilized on iron oxide-chitosan modified halloysite-nanotubes. </LI> <LI> Immobilized laccase retained the significant anti-proliferative potential. </LI> <LI> Laccase was anti-proliferative to cells with or without the estrogen-receptors. </LI> <LI> Immobilized laccase can be further developed as potential anti-cancer drug. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
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