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Wyszukujesz frazę "Olejnik, Kamil" wg kryterium: Autor


Wyświetlanie 1-4 z 4
Tytuł:
The influence of selected process factors on the physicochemical and biological properties of honeys: A review
Autorzy:
Kowalska, Gabriela
Rosicka-Kaczmarek, Justyna
Olejnik, Tomasz P.
Dędek, Kamil
Powiązania:
https://bibliotekanauki.pl/articles/410394.pdf
Data publikacji:
2019
Wydawca:
Politechnika Łódzka. Wydawnictwo Politechniki Łódzkiej
Tematy:
honey
Maillard reaction
hydroxymethylfurfural
antioxidant activity
heating
miód
reakcja Maillarda
hydroksymetylofurfural
aktywność antyoksydacyjna
ogrzewanie
Opis:
Honey is one of the world's most valued natural food products. Characteristic, pleasant aroma, golden colour, sweet taste and healthpromoting properties cause a continuous increase of honey consumption in the European Union. The most wanted is regional honey. However, imported honey available on the market has often lower prices. The honey obtained can be heat treated, which reduces water content and can slow down the growth of the microorganisms, which are responsible for the undesirable fermentation of honey. Unprocessed honey appears to be the healthiest, but in practice, it’s often heat treated to slow down or back up the crystallization process and to make its dosage during technical processes easier. It is widely believed that heating of honey may have a harmful impact on its properties. There are countless articles of popular science, that warn of heating and cooking with honey. Should honey never be heated? The aim of this work is to give an overview of the influence of technical processes on the physicochemical and health-promoting properties of honey. The results demonstrated that the physicochemical and bioactive properties of honey are significantly affected by thermal treatment. As a result of the temperature, it comes to the Maillard reaction, during which HMF is synthesized. Furthermore, heating affects the activity of the enzymes contained in honey, among others, diastase and inverses. However, few studies made in this field show that honey heat treatment may work in favour of antioxidant properties. Depending on the type of honey, melanoidins may increase or decrease the antioxidant activity.
Źródło:
Biotechnology and Food Science; 2019, 83, 1; 57-69
2084-0136
2299-6818
Pojawia się w:
Biotechnology and Food Science
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and Ggamma subunits of the signal transducing heterotrimeric G protein
Autorzy:
Olejnik, Kamil
Bucholc, Maria
Anielska-Mazur, Anna
Lipko, Agata
Kujawa, Martyna
Modzelan, Marta
Augustyn, Agnieszka
Kraszewska, Elzbieta
Powiązania:
https://bibliotekanauki.pl/articles/1039863.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein complexes
Nudix
AtNUDT7
Arabidopsis thaliana
heterotrimeric G protein
RACK1A
Opis:
Arabidopsis thaliana AtNUDT7 Nudix pyrophosphatase hydrolyzes NADH and ADP-ribose in vitro and is an important factor in the cellular response to diverse biotic and abiotic stresses. Several studies have shown that loss-of-function Atnudt7 mutant plants display many profound phenotypes. However the molecular mechanism of AtNUDT7 function remains elusive. To gain a better understanding of this hydrolase cellular role, proteins interacting with AtNUDT7 were identified. Using AtNUDT7 as a bait in an in vitro binding assay of proteins derived from cultured Arabidopsis cell extracts we identified the regulatory protein RACK1A as an AtNUDT7-interactor. RACK1A-AtNUDT7 interaction was confirmed in a yeast two-hybrid assay and in a pull-down assay and in Bimolecular Fluorescence Complementation (BiFC) analysis of the proteins transiently expressed in Arabidopsis protoplasts. However, no influence of RACK1A on AtNUDT7 hydrolase catalytic activity was observed. In vitro interaction between RACK1A and the AGG1 and AGG2 gamma subunits of the signal transducing heterotrimeric G protein was also detected and confirmed in BiFC assays. Moreover, association between AtNUDT7 and both AGG1 and AGG2 subunits was observed in Arabidopsis protoplasts, although binding of these proteins could not be detected in vitro. Based on the observed interactions we conclude that the AtNUDT7 Nudix hydrolase forms complexes in vitro and in vivo with regulatory proteins involved in signal transduction. Moreover, we provide the initial evidence that both signal transducing gamma subunits bind the regulatory RACK1A protein.
Źródło:
Acta Biochimica Polonica; 2011, 58, 4; 609-616
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mutational analysis of the AtNUDT7 Nudix hydrolase from Arabidopsis thaliana reveals residues required for protein quarternary structure formation and activity
Autorzy:
Olejnik, Kamil
Płochocka, Danuta
Grynberg, Marcin
Goch, Grażyna
Gruszecki, Wiesław
Basińska, Teresa
Kraszewska, Elżbieta
Powiązania:
https://bibliotekanauki.pl/articles/1040587.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
dimer
Nudix
structure-function analysis
mutagenesis
AtNUDT7
Arabidopsis thaliana
14.3.3 interaction
biophysical analysis
Opis:
Arabidopsis thaliana AtNUDT7, a homodimeric Nudix hydrolase active on ADP-ribose and NADH, exerts negative control on the major signaling complex involved in plant defense activation and programmed cell death. The structural and functional consequences of altering several amino-acid residues of the AtNUDT7 protein have been examined by site-directed mutagenesis, far-UV circular dichroism (CD), attenuated total reflection-Fourier transform infrared (ATR-FTIR) and photon correlation (PCS) spectroscopy, biochemical analysis and protein-protein interaction studies. Alanine substitutions of F73 and V168 disallowed dimer formation. Both the F73A- and V168A-mutated proteins displayed no observable enzymatic activity. Alanine substitution of the V69 residue did not significantly alter the enzyme activity and had no influence on dimer arrangement. The non-conserved V26 residue, used as a negative control, did not contribute to the enzyme quaternary structure or activity. Detailed biophysical characterization of the wild-type and mutant proteins indicates that the mutations do not considerably alter the secondary structure of the enzyme but they affect dimer assembly. In addition, mutating residues V69, F73 and V168 disrupted the binding of AtNUDT7 to the regulatory 14.3.3 protein. These are the first studies of the structure-function relationship of AtNUDT7, a Nudix hydrolase of important regulatory function.
Źródło:
Acta Biochimica Polonica; 2009, 56, 2; 291-300
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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