Immobilization of lipase from Candida rugosa on a polymer support

Mojović, Ljiljana; Knežević, Zorica; Popadić, Ranko; Jovanović, Slobodan

doi:10.1007/s002530051350

Cited by 40 publications

(26 citation statements)

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“…The marginally lower V max values for immobilized enzyme suggest that the activity of immobilized xylanase was not affected drastically during the course of immobilization (Table 2). However, decrease in immobilized enzyme activity observed may be due to the binding of matrices to enzyme-active site, conformational change, or the new local environment formed [35]. The increase in K m value and decrease in V max following immobilization have also been reported earlier by many investigators [15,25,36,37].…”

Section: Effect Of Substrate Concentration On Activity Of Free and Immentioning

confidence: 71%

Immobilization of Xylanase from Bacillus pumilus Strain MK001 and its Application in Production of Xylo-oligosaccharides

Kapoor

Kuhad

2007

Appl Biochem Biotechnol

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The aim of this study was to overexpress the xylanase II gene of Trichoderma reesei in Escherichia coli and determine the characteristics of the recombinant enzyme. Recombinant xylanase II gene was constructed by ligating the cDNA of xylanase, obtained from reverse transcriptase-polymerase chain reaction, and fused with NusA protein of pET-431b plasmid. An Ni2+-NTA affinity column was used to further purify the recombinant xylanase II. The molecular mass of the recombinant enzyme measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was approx 76 kDa (including 55 kDa of NusA and 21 kDa of xylanase II), and the isoelectric point and specific activity were 7.5 and 225 U/mg, respectively. The optimal reaction temperature and pH for the recombinant enzyme were 50 degrees C and 4.0, respectively. The recombinant enzyme was stable at a pH range of 5.0-10.0 and maintained 95% residual activity after incubating at 30-35 degrees C for 30 min. The kinetic parameters KM and Vmax of the recombinant xylanase II were 13.8 mg/mL and 336 micromol/(mg.min), respectively, using birchwood xylan as the substrate.

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Section: Effect Of Substrate Concentration On Activity Of Free and Immentioning

confidence: 71%

Immobilization of Xylanase from Bacillus pumilus Strain MK001 and its Application in Production of Xylo-oligosaccharides

Kapoor

Kuhad

2007

Appl Biochem Biotechnol

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“…To fully exploit the technical and economical advantages of lipases, it is recommended to use them in an immobilized form to reduce the cost and poor stability of free lipase [4][5][6][7][8][9]. Recently hybrid membranes have been prepared from the ultrafiltration of a gelatin solution onto an α-alumina macroporus ceramic support [4].…”

Section: Introductionmentioning

confidence: 99%

The wetting and interfacial properties of alumina surface treated with dipalmitoylphosphatidylcholine and lipase enzyme

Wiącek

2011

Powder Technology

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“…7). This stability is even better than that reported for lipase covalently immobilized to chitosan beads (80% activity retained after five runs; Hung et al, 2003), lipase immobilized on zeolite (31% retention of activity; Knezevic et al, 1998), and lipase immobilized by adsorption on macroporous copolymer (56% retention of activity; Mojovic et al, 1998).…”

Section: Operational Stability Of Immobilized Lipasementioning

confidence: 51%

A novel reactive perstraction system based on liquid‐core microcapsules applied to lipase‐catalyzed biotransformations

Wyss¹,

Stockar²,

Marison³

2005

Biotech & Bioengineering

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A novel reactive perstraction system has been developed based on liquid-core capsules, involving an enzyme-catalyzed reaction coupled with simultaneous in situ product recovery. Lipase-catalyzed reactions, hydrolysis of triprionin and nitrophenyl laurate, were selected to test the system and demonstrate the feasibility of immobilization of enzymes to the membranes of liquid-core capsules and the ability to extract hydrophobic products of the reaction within the capsule core. The lipase from Candida rugosa was immobilized to the microcapsules by adsorption and by covalent binding through activation with glutaraldehyde. In both cases improved temperature and operational stability were achieved. Both types of immobilization resulted in a basic shift of the pH optimum for activity, from 7.5 to 9.0. The presence of an organic phase within the capsule core allowed direct product separation and lead to a decrease in product inhibition of the lipase-catalyzed reaction.

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Immobilization of lipase from Candida rugosa on a polymer support

Cited by 40 publications

References 0 publications

Immobilization of Xylanase from Bacillus pumilus Strain MK001 and its Application in Production of Xylo-oligosaccharides

Immobilization of Xylanase from Bacillus pumilus Strain MK001 and its Application in Production of Xylo-oligosaccharides

The wetting and interfacial properties of alumina surface treated with dipalmitoylphosphatidylcholine and lipase enzyme

A novel reactive perstraction system based on liquid‐core microcapsules applied to lipase‐catalyzed biotransformations

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