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- 저자 : Lobarzewski, Jerzy (검색결과 4 건)
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An Immobilization of Extracellular Laccase to Humus - Iron Complex
Cho, Nam Seok,Leonowicz, Andrzej,Ginalska, Grazyna,Lobarzewski, Jerzy,Piccolo, Alessandro 한국목재공학회 2001 목재공학 Vol.29 No.3
There are some evidence that active enzymatic proteins, e.g. fungal laccase, exist in the naturally occured soil humus. This study was performed to investigate the covalent binding of fungal lactase to the humic acid-iron complex, and to measure lactase activity of immobilized ones. Seven methods were adopted to form the covalent binding of fungal lactase with soil humic acids complexed with iron. Using these seven methods it was possible to change the dimension of spacer arm between lactase and support, and also to regulate the mode of covalent binding of this enzyme. The spacer arm was regulated from 2C to 11C. There was not observed any straight relationship between the spacer arm longitude and the lactase activity after immobilization, but the binding mode more effective than the former. Three out of the seven methods gave the high activity of immobilized lactase, and which active products of lactase immobilization was stable up to 10 days after the process. It is indicated that natural soil condition might be prevented the lactase activation by the toxic influence of some phenolic humic compounds. It was shown, for the first time, the possibilities to obtain the high activity of fungal lactase by binding to humic acids, and especially in complex with iron.
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Purification of the Candida utilis Extracellular Invertase using Affinity Chromatography
G.Ginalska,조남석,A.Belcarz,J.Lobarzewski,A.Leonowicz 한국목재공학회 2002 목재공학 Vol.30 No.3
The extracellular invertase (EC 3.2.1.26) (Candida utilis) preparation was obtained from the liquid medium after desalting and freeze drying. This prepared enzyme was used for the comparative purification on 4 activated matrices by liquid column affinity chromatography method. In this method there were used controlled porous glass (CPG) silanized covalently activated by keratin, silanized silica gel and silica gel covalently covered by keratin. It was found that the invertase purification process was better using both CPG matrices (silanized CPG and keratin activated CPG) than these with two silica gel supports. Also the elution coefficient of the invertase from the two CPG columns was about 93 to 94%. Two silica gel supports found to be superior in terms of purification efficiency. The invertase purification process was confirmed by PAGE electrophoresis.
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Immobilization of Fungal Laccase on Keratin - Coated Soil and Glass Matrices
Cho, Nam Seok,Choi, T. H.,Jaszek, M.,Leonowicz, A.,Ginalska, G.,Lobarzewski, J.,Ohga, S. 한국목재공학회 2001 목재공학 Vol.29 No.3
Laccase enzymes from Cerrena unicolor and Trametes versicolor were immobilized on the activated glass beads (CPG), silica gel (SG) and soil (SL). The heterogeneous matrices were activated by γ-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA), and their surfaces were coated by keratin (KER) on activated or non-activated CPG, SG and SL. The laccase activities were tested in the aqueous solution for the native and immobilized preparations using different pH and temperature conditions. By keratin coating on supports, in the cases of CPG-KER and SL-KER, the immobilization yield was increased from about 80% to 90%. Moreover, much less protein was immobilized in keratin coated matrices than in inorganic ones alone (e.g. on CPG-KER 57.6%, whereas on CPG alone 80.6%). Laccase immobilization on keratin coated inorganic matrices was generally more effective than that of non-coated matrices. Concerned to pH dependency, the optima pH for immobilized laccases generally shifted towards to higher values, 5.5-5.8 and even 5.9 in the case of keratin for C. unicolor and from 5.3 to 5.7 for T. versicolor, respectively, and decreased less gradually both in acidic and alkaline regions. The immobilized laccase was more stable against thermal denaturation. This seems particularly true at 75℃ in the case of C. unicolor, where the activity of immobilized enzyme is $gt; 50% higher than that of the free enzyme. For T. versicolor the respective values were 65℃, and 50%.
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Cho, Nam Seok,Lee, S. S.,Grzywnowicz, K.,Malarczyk, E.,Leonowicz, A.,Rogalski, J.,Ginalska, G.,Lobarzewski, J.,Ohga, S.,Pashenova, N. 한국목재공학회 2000 목재공학 Vol.28 No.4
Highly purified Cerrena unicolor laccase (benzenediol:oxygen oxidoreductase, EC 1.10.3.2) caused the demethoxylation of milled wood lignin and several lignin related substances. The constitutive form of the enzyme produced extracellularly by C. unicolor fermenter culture was isolated and purified by ion-exchange chromatography on the DEAE-Toyopearl column and by affinity chromatography on a ConA-Sepharose and Syringyl-AH-Sepharose 4B columns. The enzyme was further immobilized on functionalized porous glass (CPG) and keratin coated CPG. The demethylating activity was monitored both by estimation of released methanol and by detection of the level of methoxyl groups (also in some water miscible solvents) after incubation of lignin materials with laccase preparations (free and immobilized). The effects of the incubation time and temperature on the demethoxylating activity of immobilized laccase preparations were also studied.
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