Studies of stabilization of native catalase using additives

Costa, Sérgio E. Gouvêa da; Tzanov, Tzanko; Carneiro, Alexandre; Paar, Andreas; Gübitz, Georg; Cavaco‐Paulo, Artur

doi:10.1016/s0141-0229(01)00505-1

Cited by 82 publications

(50 citation statements)

References 15 publications

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“…Stabilizing an enzyme normally means suppressing the unfolding of the protein and retaining the catalytic activity [1]. Stabilization of enzymes could be achieved by modifi cation of the protein structure by protein engineering, chemical modifi cation or by immobilization [2]. The enzymes that can withstand extreme conditions can be isolated from extremophiles.…”

Section: Introductionmentioning

confidence: 99%

“…The enzymes that can withstand extreme conditions can be isolated from extremophiles. The stabilization can be achieved by the addition of additives like substrates, products, inhibitors, cofactors, metal ions, proteins, sugars and natural or synthetic polymers [1][2][3][4][5]. The use of enzymes for industrial purposes usually depends on their stability during isolation, purifi cation and storage [3].…”

Section: Introductionmentioning

confidence: 99%

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Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

2010

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Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640 with various stabilizers at different temperatures was studied. Dextransucrase was stable at lower temperatures (10-30°C) and lost the activity at above 30°C. The salts such as CaCl 2 , CoCl 2 and MgCl 2 enhanced the dextransucrase activity. A 22% higher dextransucrase activity was obtained by 4 mM CoCl 2 . The dextransucrase activity was lost by 50% at 1 mM EDTA. Urea denatured the enzyme and caused 45%, 90% and 98% loss of activity in 30 min when treated with 1 M, 3 M, and 5 M urea concentrations, respectively. Amongst the stabilizers Tween 80, glycerol, PEG-8000, dextran (500 kDa) and glutaraldehyde, Tween 80 provided the maximum stability at 30°C. In the presence of Tween 80 the enzyme lost only 8% activity at 30°C in 20 h but, it lost 65% of activity with out any stabilizer. The enzyme lost 92% of activity with in 4 days at 30°C and lost only 25% of activity at -20°C after 14 days.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

2010

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“…The process of HPD by the catalase in industrial practice undergoes at low substrate concentrations (Costa et al, 2002b;Deluca et al, 1995;Tarhan and Telefoncu, 1990;Tarhan and Uslan, 1990;Tarhan, 1995;Vasudevan and Weiland, 1990;Vasudeven and Weiland, 1993). Thus, a relationship between the reaction rate, rA, and the substrate (hydrogen peroxide) concentration in the bioreactor (at the fixed activity of catalase) is given by…”

Section: Apparent Reaction Ratementioning

confidence: 99%

External Mass Transfer Model for Hydrogen Peroxide Decomposition by Terminox Ultra Catalase in a Packed-Bed Reactor

Grubecki¹

2017

Chemical and Process Engineering

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It is known that external diffusional resistances are significant in immobilized enzyme packed-bed reactors, especially at large scales. Thus, the external mass transfer effects were analyzed for hydrogen peroxide decomposition by immobilized Terminox Ultra catalase in a packed-bed bioreactor. For this purpose the apparent reaction rate constants, kP, were determined by conducting experimental works at different superficial velocities, U, and temperatures. To develop an external mass transfer model the correlation between the Colburn factor, JD, and the Reynolds number, Re, of the type JD = K Re (n-1) was assessed and related to the mass transfer coefficient, kmL. The values of K and n were calculated from the dependence (am kp) vs. Re -1 making use of the intrinsic reaction rate constants, kR, determined before. Based on statistical analysis it was found that the mass transfer correlation JD = 0.972 Re -0.368 predicts experimental data accurately. The proposed model would be useful for the design and optimization of industrial-scale reactors.

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“…Surfactants may facilitate the transfer of hydrophobic substrate through the layer of water molecules to the enzyme-binding site (Khalaf et al 1996). Costa et al 2002 studied the storage stability of native catalase treated with different additives at stress conditions, i.e.. pH 10 -12, and 60 and 70ºC. At pH 10 and 11 the glycerol was the only additive to improve the enzyme stability.…”

Section: Effect Of Ionic and Non-ionic Additives In The Textile Bathsmentioning

confidence: 99%

“…The spacer molecule gives a greater degree of mobility to the coupled biocatalyst so that its activity can, under certain circumstances, be higher than if it is bound directly to the support. Costa et al 2002 studied also the effect of different surfactants and peroxide stabilizing agents present in the bleaching liquor on the activity of immobilized catalase. Some anionic surfactant (C 10 -C 13 ) reduced the activity of the immobilized enzyme by 96%.…”

Section: Effect Of Immobilization On Enzyme Activitymentioning

confidence: 99%

Protein interactions in enzymatic processes in textiles

Tzanov¹,

Andreaus²,

Guebitz³

et al. 2003

Electron. J. Biotechnol.

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Enzymes are the catalysts of all reactions in living systems. These reactions are catalysed in the active sites of globular proteins. The proteins are composed by amino acids with a variety of side chains ranging from non-polar aliphatic and aromatic to acidic, basic and neutral polar. This fact allows to a globular 3D protein to create in the active site all ranges of microenvironments for catalysis. Major advances in microbial technology and genetics allow recently the broad range of enzymatic applications in the industry. Enzymatic processes have been increasingly incorporated in textiles over the last years. Cotton, wool, flax or starches are natural materials used in textiles that can be processed with enzymes. Enzymes have been used for desizing, scouring, polishing, washing, degumming, peroxide degradation in bleaching baths as well as for decolourisation of dyehouse wastewaters, bleaching of released dyestuff and inhibiting dye transfer. Furthermore many new applications are under development such as natural and synthetic fibres modification, enzymatic dyeing, finishing etc. Most of the textile processes are heterogeneous where an auxiliary as a dye, enzyme, softener or oxidant have to *Corresponding author be taken from the solution to the fibre. These processes require the presence of surface-active agents, ionic force "balancers", buffers, stabilisers and others, and are characterized with high turbulence and mechanical agitation in the textile baths. In this paper it is intended to understand and discuss the major protein interactions within textile processes and to try to anticipate troubleshooting possibilities when enzymes are used. It can be expected that an enzyme protein can interact with all chemical agents in solution due to the large variety of side chains of the outer-amino-acids in the large 3D structure of the protein. Without the aim of being exhaustive various points will be discussed where protein interactions are important for textile processing.

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Studies of stabilization of native catalase using additives

Cited by 82 publications

References 15 publications

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

External Mass Transfer Model for Hydrogen Peroxide Decomposition by Terminox Ultra Catalase in a Packed-Bed Reactor

Protein interactions in enzymatic processes in textiles

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