This HTML5 document contains 61 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Namespace Prefixes

PrefixIRI
dctermshttp://purl.org/dc/terms/
n18http://localhost/temp/predkladatel/
n11http://linked.opendata.cz/resource/domain/vavai/projekt/
n4http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n14http://linked.opendata.cz/resource/domain/vavai/subjekt/
n13http://linked.opendata.cz/ontology/domain/vavai/
shttp://schema.org/
skoshttp://www.w3.org/2004/02/skos/core#
n3http://linked.opendata.cz/ontology/domain/vavai/riv/
n17http://bibframe.org/vocab/
n2http://linked.opendata.cz/resource/domain/vavai/vysledek/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n10http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F61989592%3A15310%2F13%3A33147923%21RIV14-AV0-15310___/
n7http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n5http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n19http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n15http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n20http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n16http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n6http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F61989592%3A15310%2F13%3A33147923%21RIV14-AV0-15310___
rdf:type
n13:Vysledek skos:Concept
dcterms:description
In this work, magnetosomes produced by microorganisms were chosen as a suitable magnetic carrier for covalent immobilization of thermostable trypsin conjugates with an expected applicability for efficient and rapid digestion of proteins at elevated temperatures. First, a biogenic magnetite was isolated from Magnetospirillum gryphiswaldense and its free surface was coated with the natural polysaccharide chitosan containing free amino and hydroxy groups. Prior to covalent immobilization, bovine trypsin was modified by conjugating with alfa-, beta- and gama-cyclodextrin. Modified trypsin was bound to the magnetic carriers via amino groups using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide and N-hydroxysulfosuccinimide as coupling reagents. The magnetic biomaterial was characterized by magnetometric analysis and electron microscopy. With regard to their biochemical properties, the immobilized trypsin conjugates showed an increased resistance to elevated temperatures, eliminated autolysis, had an unchanged pH optimum and a significant storage stability and reusability. Considering these parameters, the presented enzymatic system exhibits properties that are superior to those of trypsin forms obtained by other frequently used approaches. The proteolytic performance was demonstrated during in-solution digestion of model proteins (horseradish peroxidase, bovine serum albumin and hen egg white lysozyme) followed by mass spectrometry. It is shown that both magnetic immobilization and chemical modification enhance the characteristics of trypsin making it a promising tool for protein digestion. In this work, magnetosomes produced by microorganisms were chosen as a suitable magnetic carrier for covalent immobilization of thermostable trypsin conjugates with an expected applicability for efficient and rapid digestion of proteins at elevated temperatures. First, a biogenic magnetite was isolated from Magnetospirillum gryphiswaldense and its free surface was coated with the natural polysaccharide chitosan containing free amino and hydroxy groups. Prior to covalent immobilization, bovine trypsin was modified by conjugating with alfa-, beta- and gama-cyclodextrin. Modified trypsin was bound to the magnetic carriers via amino groups using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide and N-hydroxysulfosuccinimide as coupling reagents. The magnetic biomaterial was characterized by magnetometric analysis and electron microscopy. With regard to their biochemical properties, the immobilized trypsin conjugates showed an increased resistance to elevated temperatures, eliminated autolysis, had an unchanged pH optimum and a significant storage stability and reusability. Considering these parameters, the presented enzymatic system exhibits properties that are superior to those of trypsin forms obtained by other frequently used approaches. The proteolytic performance was demonstrated during in-solution digestion of model proteins (horseradish peroxidase, bovine serum albumin and hen egg white lysozyme) followed by mass spectrometry. It is shown that both magnetic immobilization and chemical modification enhance the characteristics of trypsin making it a promising tool for protein digestion.
dcterms:title
Thermostable trypsin conjugates immobilized to biogenic magnetite show a high operational stability and remarkable reusability for protein digestion Thermostable trypsin conjugates immobilized to biogenic magnetite show a high operational stability and remarkable reusability for protein digestion
skos:prefLabel
Thermostable trypsin conjugates immobilized to biogenic magnetite show a high operational stability and remarkable reusability for protein digestion Thermostable trypsin conjugates immobilized to biogenic magnetite show a high operational stability and remarkable reusability for protein digestion
skos:notation
RIV/61989592:15310/13:33147923!RIV14-AV0-15310___
n13:predkladatel
n14:orjk%3A15310
n3:aktivita
n19:S n19:P
n3:aktivity
P(ED0007/01/01), P(ED2.1.00/03.0058), P(EE2.3.20.0155), P(KAN115600801), P(LH12085), S
n3:cisloPeriodika
12
n3:dodaniDat
n6:2014
n3:domaciTvurceVysledku
n4:8402566 n4:2612526 n4:5341620 n4:9708790 n4:2176645 n4:7008686 n4:9251189
n3:druhVysledku
n20:J
n3:duvernostUdaju
n5:S
n3:entitaPredkladatele
n10:predkladatel
n3:idSjednocenehoVysledku
110975
n3:idVysledku
RIV/61989592:15310/13:33147923
n3:jazykVysledku
n15:eng
n3:klicovaSlova
biogenic magnetite, chitosan, immobilization, MALDI-TOF, proteomics, stability, trypsin
n3:klicoveSlovo
n7:MALDI-TOF n7:biogenic%20magnetite n7:proteomics n7:trypsin n7:stability n7:immobilization n7:chitosan
n3:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n3:kontrolniKodProRIV
[85A901C8482F]
n3:nazevZdroje
Nanotechnology
n3:obor
n16:CE
n3:pocetDomacichTvurcuVysledku
7
n3:pocetTvurcuVysledku
7
n3:projekt
n11:KAN115600801 n11:ED0007%2F01%2F01 n11:ED2.1.00%2F03.0058 n11:LH12085 n11:EE2.3.20.0155
n3:rokUplatneniVysledku
n6:2013
n3:svazekPeriodika
24
n3:tvurceVysledku
Poláková, Kateřina Čuda, Jan Zbořil, Radek Marková, Zdenka Pečová, Michaela Šafářová, Klára Šebela, Marek
n3:wos
000315929400002
s:issn
0957-4484
s:numberOfPages
11
n17:doi
10.1088/0957-4484/24/12/125102
n18:organizacniJednotka
15310