Improved catalytic hydrolysis of carboxy methyl cellulose using cellulase immobilized on functionalized meso cellular foam

Kannan, K.; Jasra, Raksh V.

doi:10.1007/s10934-010-9392-2

Cited by 19 publications

(14 citation statements)

References 33 publications

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“…Some immobilization protocols can modify enzyme activity and increase the enzyme stability against denaturing agents such as pH, temperature, oxygen, reactants, and proteases . In addition, the immobilization is considered industrially favorable, since allows continuous processes, for example, when used in fixed reactors . However, the immobilization procedure choice is important to avoid uncontrolled enzyme‐support interactions, which could reduce the substrate access to the active site .…”

Section: Introductionmentioning

confidence: 99%

“…1,3 In addition, the immobilization is considered industrially favorable, since allows continuous processes, for example, when used in fixed reactors. 4 However, the immobilization procedure choice is important to avoid uncontrolled enzymesupport interactions, which could reduce the substrate access to the active site. 5 Several immobilization techniques such as physical adsorption, entrapment, and covalent binding have been used on different supports to allow the industrial application of these enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

Gennari

Mobayed

Rafael

et al. 2018

Biotechnology Progress

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We studied the modification of Immobead 150 support by either introducing aldehyde groups using glutaraldehyde (Immobead-Glu) or carboxyl groups through acid solution (Immobead-Ac) for enzyme immobilization by covalent attachment or ion exchange, respectively. These two types of immobilization were compared with the use of epoxy groups that are now provided on a commercial support. We used Aspergillus oryzae β-galactosidase (Gal) as a model protein, immobilizing it on unmodified (epoxy groups, Immobead-Epx) and modified supports. Immobilization yield and efficiency were tested as a function of protein loading (10-500 mg g support). Gal was efficiently immobilized on the Immobeads with an immobilization efficiency higher than 75% for almost all supports and protein loads. Immobilization yields significantly decreased when protein loadings were higher than 100 mg g support. Gal immobilized on Immobead-Glu and Immobead-Ac retained approximately 60% of its initial activity after 90 days of storage at 4°C. The three immobilized Gal derivatives presented higher half-lifes than the soluble enzyme, where the half-lifes were twice higher than the free Gal at 73°C. All the preparations were moderately operationally stable when tested in lactose solution, whey permeate, cheese whey, and skim milk, and retained approximately 50% of their initial activity after 20 cycles of hydrolyzing lactose solution. The modification of the support with glutaraldehyde provided the most stable derivative during cycling in cheese whey hydrolysis. Our results suggest that the Immobead 150 is a promising support for Gal immobilization. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:934-943, 2018.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

Gennari

Mobayed

Rafael

et al. 2018

Biotechnology Progress

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“…Recently, the immobilization of enzymes onto mesoporous siliceous foams (MCFs) has been established . MCF is composed of a disordered pore system consisting of cage‐like pores (20–50 nm), which are cross‐linked by smaller windows (9–26 nm) .…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Alcohol Dehydrogenase from E. coli onto Mesoporous Silica for Application as a Cofactor Recycling System

Dreifke

Fröba

2017

ChemCatChem

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What intrigues you about the immobilization of enzymes? Enzymes are fascinating biocatalysts with ar emarkable three-dimensionals tructure. Prior to the immobilization of an enzyme,i ti sn ecessary to carefullyi nvestigate its response when applying different pH values, diverse ionic strengthso r variouss ubstrates. Herebyaconsistent and comprehensive view of the respective enzymei so btained progressively,w hich contributest ou nderstand the behavior of an immobilized enzyme.I ti si mpressive that an enzyme confined in nanopores retains its enzymatic activity. Why are mesoporouss ilicasp romising host materials for enzymes in general? The pore size of mesoporous silicas and their surface properties can be individually tailored according to the requirements of the respective enzyme. Hence, mesoporous silicas are versatile support materials. Furthermore, the syntheses of mesopo-rous silicas are well understood and are highly reproducible. Therefore, ac onstant quality of the support material can be guaranteed. Is the immobilizationo fe nzymes aseminal approach? Enzymes catalyze countless reactions in nature. Severalo f these reactions are used in laboratory as well as industrial scale. Additionally,n umerous enzymesa re knownt op ossess ab road substrate specificity,w hich enables them to convert substrates of non-natural origin too. Immobilization ensures re-usabilityo ft he enzyme. Thus, the high costs of an enzymatic catalytic route can be relativized and the advantageso f enzyme catalysis can be used to their full extent. The front cover artworkf or Issue 7/2017 is provided by M. Dreifke, F. J. Brieler and M. Frçba,U niversity of Hamburg. The image shows as ingle spherical cell of am esoporous cellular siliceous foam with an immobilized alcohol dehydrogenase (ADH).T he ADH is able to catalyze the oxidationo f2-propanol to acetone with concomitant reduction of NADP + + to NADPH. However,i nt he presence of as ufficient concentration of acetone, the back reactiona ccompanied by the oxidation of NADPH to NADP + + can be introduced too. See the Full Paper itself at http://dx.

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“…Many methods have been used for the degradation of cellulosic materials to sugars, such as acidolysis (Li et al, 2010), alkaline hydrolysis (Carrillo et al, 2005) and enzymatic hydrolysis (Park et al, 2002). Among these methods, the enzymatic hydrolysis has received great attention due to the fact that the enzymatic process has the potential to convert the lignocellulosic materials to ethanol with a high yield and low production cost (Wingren et al, 2003;Galbe and Zacchi, 2002;Kannan and Jasra, 2011). However, the cost of ethanol production from lignocellulosic materials is relatively high based on current enzymatic hydrolysis technologies, and the main challenges are the low yield and high cost of the hydrolysis process (Sun and Cheng, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…However, the cost of ethanol production from lignocellulosic materials is relatively high based on current enzymatic hydrolysis technologies, and the main challenges are the low yield and high cost of the hydrolysis process (Sun and Cheng, 2002). The difficulties above can be partly overcome by the immobilization of cellulase due to the fact that celulase can be reused while retaining its specificity and stability (Kannan and Jasra, 2011). The capacity to retain or recover enzymes also allows biocatalyst separation from product, thereby permitting continuous processes, and prevents carrythrough of protein or activity to subsequent process steps (Polizzi et al, 2007;Brady and Jordaan, 2009).…”

Section: Introductionmentioning

confidence: 99%

Immobilization of cellulase on modified mesoporous silica shows improved thermal stability and reusability

Yin¹,

Su²,

Shao³

et al. 2013

Afr. J. Microbiol. Res.

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Cellulase was covalently immobilized using modified mesoporous silica as carrier, and the characters of immobilized cellulase were investigated including the optimum pH, the optimum temperature, thermal stability, reusability, storage stability and enzyme kinetics. As compared to the free enzyme, the optimum pH of the immobilized cellulase showed no changes, the optimum temperature showed a slight increase to 60°C. The immobilized enzymes demonstrated enhanced thermal stability, while the free enzymes lost almost 40% initial activity, the immobilized forms lost only 9% initial activity within a period of 120 min at 60°C. The immobilized cellulase showed excellent reusability. After 11 cycles, the cellulase immobilized on modified mesoporous silica still retained 89% of its initial activity. At optimized conditions, Km and Vmax values for the immobilized enzyme were slightly increased when compared with those of free enzyme. The characters of cellulase immobilized on modified mesoporous silica suggest that the immobilized enzyme has high potential for application in the industrial degradation of cellulose.

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Improved catalytic hydrolysis of carboxy methyl cellulose using cellulase immobilized on functionalized meso cellular foam

Cited by 19 publications

References 33 publications

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

Modification of Immobead 150 support for protein immobilization: Effects on the properties of immobilized Aspergillus oryzae β‐galactosidase

Immobilization of Alcohol Dehydrogenase from E. coli onto Mesoporous Silica for Application as a Cofactor Recycling System

Immobilization of cellulase on modified mesoporous silica shows improved thermal stability and reusability

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