Preparation and characterization of Rhizopus amyloglucosidase immobilized on poly(o-toluidine)

Ashly, P.C.; Mohanan, Pezholil

doi:10.1016/j.procbio.2010.04.022

Cited by 11 publications

(14 citation statements)

References 26 publications

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“…Cu ion chelated with FeSBA-15-PGMA@imidazole shows similar results in reusability studies was reported by Zaho et al [28]. It has been reported that salt and base forms of poly (o-toluidine) retained 80-85% of initial activity after 8 cycles [29].…”

Section: Reusability Of Immobilized Enzymesupporting

confidence: 83%

“…The 29 Si MAS spectrum of the MS exhibits two resonance peaks at -100.54 ppm for Q 3 environment with a shoulder at -91.38 ppm responsible for Q 2 environment. It is observed (Fig.…”

Section: Si Mas Spectral Studiesmentioning

confidence: 99%

“…Nitrogen physisorption measurements were done in a Micromeritics Tri-Star 3000 surface area and porosity analyzer (degassing conditions -N2 atmosphere, 200 ⁰C for MS, and room temperature for other samples, time 12 h). Si environment of the samples were analyzed by 29 Si MAS solid state NMR. These experiments were carried out over a Bruker DSX-300 spectrometer at a resonance frequency of 78.1 MHz (sample spinning frequency was 8 kHz, 10 ms pulse length, pulse delay 2 s and number of scans 1024) and tetra methyl silane is used as internal standard.…”

Section: Characterization Of Meso Silica Functionalized and Immobilimentioning

confidence: 99%

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Improved Stabilities of Immobilized Glucoamylase on Functionalized Mesoporous Silica Synthesised using Decane as Swelling Agent

George

Gopinath

Sugunan

2013

Bull. Chem. React. Eng. Catal.

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Ordered mesoporous silica, with high porosity was used to immobilize glucoamylase via adsorption and covalent binding. Immobilization of glucoamylase within mesoporous silica was successfully achieved, resulting in catalytically high efficiency during starch hydrolysis. In this study, mesoporous silica was functionalized by co-condensation of tetraethoxysilane (TEOS) with organosilane (3-aminopropyl) triethoxysilane (APTES) in a wide range of molar ratios of APTES: TEOS in the presence of triblock copolymer P123 under acidic hydrothermal conditions. The prepared materials were characterized by Small angle XRD, Nitrogen adsorption -desorption and 29 Si MAS solid state NMR. N2 desorption studies showed that pore size distribution decreases due to pore blockage after functionalization and enzyme immobilization. Small angle XRD and 29 Si MAS NMR study reveals mesophase formation and Si environment of the materials. The main aim of our work was to study the catalytical activity, effect of pH, temperature, storage stability and reusability of covalently bound glucoamylase on mesoporous silica support. The result shows that the stability of enzyme can be enhanced by immobilization.

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Section: Reusability Of Immobilized Enzymesupporting

confidence: 83%

“…The 29 Si MAS spectrum of the MS exhibits two resonance peaks at -100.54 ppm for Q 3 environment with a shoulder at -91.38 ppm responsible for Q 2 environment. It is observed (Fig.…”

Section: Si Mas Spectral Studiesmentioning

confidence: 99%

Section: Characterization Of Meso Silica Functionalized and Immobilimentioning

confidence: 99%

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Improved Stabilities of Immobilized Glucoamylase on Functionalized Mesoporous Silica Synthesised using Decane as Swelling Agent

George

Gopinath

Sugunan

2013

Bull. Chem. React. Eng. Catal.

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“…It is used in the form of poly(hydroxybutyrate) nanoparticles (Deepak et al 2009) and small or large poly(hydroxybutyrate) beads (Mendes et al 2011). Another carrier, poly(o-toluidine) built of particles of o-toluidine isomer has active -NH 2 groups (Ashly and Mohanan 2010). Furthermore, poly(acrylonitrile) (PAN), a polymer widely used in the production of synthetic fibres, as an enzyme carrier is used in the form of electrospun fibres (Sakai et al 2010).…”

Section: Organic Carriersmentioning

confidence: 99%

Enzyme immobilization by adsorption: a review

2014

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Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes' low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.

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“…This optimum temperature was similar to temperatures from other reported Rhizopus sp. (45-55 o C) (21,22) while thermostable glucoamylases from Chaetomium thermophilum and Aspergillus niger exhibited high optimum temperatures (65-70 o C) (9,23).…”

Section: Resultsmentioning

confidence: 99%

Characterization of the starch degradation activity from newly isolated Rhizopus oryzae WCS-1 and mixed cultures with Saccharomyces cerevisiae for efficient ethanol production from starch

Jang

Kim

Park

et al. 2015

Food Sci Biotechnol

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Preparation and characterization of Rhizopus amyloglucosidase immobilized on poly(o-toluidine)

Cited by 11 publications

References 26 publications

Improved Stabilities of Immobilized Glucoamylase on Functionalized Mesoporous Silica Synthesised using Decane as Swelling Agent

Improved Stabilities of Immobilized Glucoamylase on Functionalized Mesoporous Silica Synthesised using Decane as Swelling Agent

Enzyme immobilization by adsorption: a review

Characterization of the starch degradation activity from newly isolated Rhizopus oryzae WCS-1 and mixed cultures with Saccharomyces cerevisiae for efficient ethanol production from starch

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