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Statements

Subject Item
n2:RIV%2F67179843%3A_____%2F14%3A00434309%21RIV15-AV0-67179843
rdf:type
skos:Concept n10:Vysledek
dcterms:description
Recombinant cyclodextrin glucanotransferase JCGT8-5 (CGTase, EC 2.4.1.19) was effectively immobilized by adsorption on magnetically-modified particles. Silicates (montmorillonite and halloysite), natural supports (oat straw, wheat bran, banana peel, sawdust, hazelnut and peanut shell, coffee beans, tea leaves, algae Chlorella vulgaris) and activated carbon were engaged as carriers, as the most of them were used for the first time for enzyme adsorption. The immobilization capacities of the carriers entrapping ultra-concentrate or purified enzyme were determined. Binding yields reached from 50% to 90% of the initial enzyme quantity. The analysis of the formed cyclodextrins (CDs) revealed that the highest amount of total CDs was obtained by the use of halloysite particles (10.1 mg/ml), followed by sawdust (8.6 mg/ml), algae (8.6 mg/ml) and peanut shell (8.2 mg/ml). A high degree of starch conversion into CDs, ranging from 21 to 25% was achieved for 20 min starch hydrolysis. Variations in γ-CD: α-CD: β-CD ratios due to the immobilization on the different carriers were observed. The six-fold reuse of the magnetic biocatalysts containing purified recombinant CGTase bound to halloysite, washed algae or sawdust provided 29-36 mg/ml CD yield without presence of α-CD for 120 min starch hydrolysis. Recombinant cyclodextrin glucanotransferase JCGT8-5 (CGTase, EC 2.4.1.19) was effectively immobilized by adsorption on magnetically-modified particles. Silicates (montmorillonite and halloysite), natural supports (oat straw, wheat bran, banana peel, sawdust, hazelnut and peanut shell, coffee beans, tea leaves, algae Chlorella vulgaris) and activated carbon were engaged as carriers, as the most of them were used for the first time for enzyme adsorption. The immobilization capacities of the carriers entrapping ultra-concentrate or purified enzyme were determined. Binding yields reached from 50% to 90% of the initial enzyme quantity. The analysis of the formed cyclodextrins (CDs) revealed that the highest amount of total CDs was obtained by the use of halloysite particles (10.1 mg/ml), followed by sawdust (8.6 mg/ml), algae (8.6 mg/ml) and peanut shell (8.2 mg/ml). A high degree of starch conversion into CDs, ranging from 21 to 25% was achieved for 20 min starch hydrolysis. Variations in γ-CD: α-CD: β-CD ratios due to the immobilization on the different carriers were observed. The six-fold reuse of the magnetic biocatalysts containing purified recombinant CGTase bound to halloysite, washed algae or sawdust provided 29-36 mg/ml CD yield without presence of α-CD for 120 min starch hydrolysis.
dcterms:title
Immobilization of Recombinant CGTase JCGT8-5 on Magnetically-Modified Silicates and Natural Supports Immobilization of Recombinant CGTase JCGT8-5 on Magnetically-Modified Silicates and Natural Supports
skos:prefLabel
Immobilization of Recombinant CGTase JCGT8-5 on Magnetically-Modified Silicates and Natural Supports Immobilization of Recombinant CGTase JCGT8-5 on Magnetically-Modified Silicates and Natural Supports
skos:notation
RIV/67179843:_____/14:00434309!RIV15-AV0-67179843
n4:aktivita
n15:I
n4:aktivity
I
n4:cisloPeriodika
1
n4:dodaniDat
n6:2015
n4:domaciTvurceVysledku
n11:3631699 n11:3082059
n4:druhVysledku
n12:J
n4:duvernostUdaju
n5:S
n4:entitaPredkladatele
n14:predkladatel
n4:idSjednocenehoVysledku
20528
n4:idVysledku
RIV/67179843:_____/14:00434309
n4:jazykVysledku
n9:eng
n4:klicovaSlova
immobilization; recombinant CGTase; magnetic carriers; CDs production
n4:klicoveSlovo
n8:immobilization n8:recombinant%20CGTase n8:CDs%20production n8:magnetic%20carriers
n4:kodStatuVydavatele
BG - Bulharská republika
n4:kontrolniKodProRIV
[2342D8DA6FF3]
n4:nazevZdroje
International Review of Chemical Engineering
n4:obor
n16:BO
n4:pocetDomacichTvurcuVysledku
2
n4:pocetTvurcuVysledku
7
n4:rokUplatneniVysledku
n6:2014
n4:svazekPeriodika
6
n4:tvurceVysledku
Tonkova, A. Ivanova, V. Petrov, K. Šafařík, Ivo Delchev, N. Šafaříková, Miroslava Petrova, P.
s:issn
2035-1755
s:numberOfPages
8