Comparison of some properties of immobilized and soluble forms of fungal peroxidase

L̷obarzewski, J.

doi:10.1002/bit.260230920

Cited by 16 publications

(3 citation statements)

References 27 publications

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“…In some earlier papers the authors did not take intO consideration the Brought to you by | University of Arizona Authenticated Download Date | 5/30/15 9:08 PM frequent occurrence of both oxidases in the fungal material (Blaich 1972;Blaich et al 1975;Kaplan 1979;Haars 1980). Peroxidase after its immobilization on glass beads was more stable and could be used several times withour losing activity (Lobarzewski 1981b). As can be seen from Figures 2 and 3 and Tables l and 2, the fungal peroxidase used in our experiments was able to change considerable the molecular weight of Na-lignosulfonates.…”

Section: Resultsmentioning

confidence: 93%

“…1979). The earlier described procedure was also used in further steps of peroxidase Separation from laccase present in this material (Lobarzewski 1981b). This method is based on affinity between fungal peroxidase and vanülin used äs a ligand attached to the silanized glass bead carrier.…”

Section: Introductionmentioning

confidence: 99%

“…This method is based on affinity between fungal peroxidase and vanülin used äs a ligand attached to the silanized glass bead carrier. The form I of peroxidase isolated using the above method was then rechromatographed on CM-cellulose column (Lobarzewski 1981b). …”

Section: Introductionmentioning

confidence: 99%

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The Effects of Fungal Peroxidase on Na-Lignosulfonates

L̷obarzewski¹,

Trojanowski²,

Wojtas-Wasilewska³

1982

Holzforschung

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Section: Resultsmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

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The Effects of Fungal Peroxidase on Na-Lignosulfonates

L̷obarzewski¹,

Trojanowski²,

Wojtas-Wasilewska³

1982

Holzforschung

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Purification and immobilization of dextranase

Rogalski

Głowiak

Szczodrak

et al. 1998

Acta Biotechnologica

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An enzymic characteristi of Novo dextranase wa presented. In addition to a high dextranolytic activity (7,200 U/ml), the crude enzyme also contained small amounts of protease, glucoamylase, polygalacturonase, carboxymethylcellulase, laminarinase and chitinase. A highly purified dextranase was then simply separated from a commercial preparation by column chromatographies on DEAESepharose. CM-Sepharose, and by chromatofocussing on Polybuffer Exchanger PBE-94. The enzyme was recovered with an over 200-fold increase in specific activity and a yield of 84%. The final preparation was homogeneous, as observed during high performance liquid chromatography (HPLC). Size-exclusion HPLC indicated that dextranase had a molecular mass of 35 kDa and its isoelectric point, established by chromatofocussing. was 4.85. Analysis of the dextran break-down products indicated that purified dextranase represents an endolytic mode of action, and isomaltose and isomaltotriose were identified as the main reducing sugars of dextran hydrolysis. The enzyme was then covalently coupled to the silanized porous glass beads modified by glutataldehyde (Carrier I) or carbodiimide (Carrier II). It was shown that immobilization of dextranase gave optimum pH and temperature ranges from 5.4 to 5.7 and from 50 "C to 60 O C . respectively. The a f f~t y of the enzyme to the substrate decreased by a factor of more than 13 for dextranase immobilized on Carrier I and increased slightly (about 1.4-times) for the enzyme bound to Carrier II.

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Dearomatization of lignin derivatives by fungal protocatechuate 3,4‐dioxygenase immobilized on porosity glass

Wojtas-Wasilewska

Luterek

Leonowicz

et al. 1988

Biotech & Bioengineering

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Protocatechuate 3,4-dioxygenase (see protocatechuate: oxygen 3,4-oxidoreductase, EC 1.13.11.3) was isolated from the mycelium of Pleurotus ostreatus (induced with p-hydroxybenzoic acid) and immobilized on controlled porosity glass beads. Four fractions of Na-lignosulfonates (varying in M(r), after chromatography on Sephadex G-50) were treated with the immobilized enzyme. The products after incubation showed the same M(r) as the untreated fractions, but their light absorption at 280 nm considerably decreased. These studies indicate that dioxygenase causes partial dearomatization of lignin macromolecule.

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Comparison of some properties of immobilized and soluble forms of fungal peroxidase

Cited by 16 publications

References 27 publications

The Effects of Fungal Peroxidase on Na-Lignosulfonates

The Effects of Fungal Peroxidase on Na-Lignosulfonates

Purification and immobilization of dextranase

Dearomatization of lignin derivatives by fungal protocatechuate 3,4‐dioxygenase immobilized on porosity glass

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