Temat: reducing capacity - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Comparison of physical-chemical properties of amylophosphoric acid and mono-starch phosphate salts
Autorzy:: Fortuna, T.
Gibinski, M.
Palasinski, M.
Powiązania:: https://bibliotekanauki.pl/articles/1371740.pdf
Data publikacji:: 1992
Wydawca:: Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:: water binding capacity
physicochemical property
paste transparency
reducing capacity
mono-starch phosphate salt
amylophosphoric acid
Źródło:: Polish Journal of Food and Nutrition Sciences; 1992, 01, 3; 119-124
1230-0322
2083-6007
Pojawia się w:: Polish Journal of Food and Nutrition Sciences
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Influence of 2,5-dichloro-1,4-benzoquinone on jack bean urease activity. Inhibitory effect, total reducing capacity and DPPH radical scavenging activity
Autorzy:: Kot, Mirosława
Olech, Zofia
Powiązania:: https://bibliotekanauki.pl/articles/1039867.pdf
Data publikacji:: 2011
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: reducing capacity
inhibition
urease
Folin-Ciocalteu method
2,5-dichloro-1,4-naphthoquinone
DPPH scavenging activity
Opis:: Inhibition of jack bean activity by 2,5-dichloro-1,4-benzoquinone (DCBQ) was studied in phosphate buffer, pH 7.0. It was found that DCBQ acted as a strong, time and concentration dependent inactivator of urease. Under the experimental conditions obeyed the terms of pseudo-first-order reaction, urease was totally inactivated. Application of Wilson-Kitz method proved that the urease-DCBQ interaction followed a simple bimolecular process and the presence of intermediate complex was undetectable. The determined second order rate constant of the inactivation was 0.053 (μM min)-1. Thiols such as l-cysteine, glutathione and dithiothreitol (DTT) protected urease from inhibition by DCBQ but DCBQ-modified urease did not regain its activity after DTT application. The thiol protective studies indicated an essential role of urease thiol(s) in the inhibition. The irreversibility of the inactivation showed that the process was a result of a direct modification of urease thiol(s) by DCBQ (DCBQ chlorine(s) substitution). The decomposition of DCBQ in aqueous solution at natural light exposure was monitored by visible spectrophotometry, determination of the total reducing capacity (Folin-Ciocalteu method) and DPPH (2,2-diphenyl-1-picrylhydrazyl) radical scavenging ability. The DCBQ conversion resulted in a decrease of the inhibition power and was well correlated with the increase of the total reducing capacity and DPPH scavenging ability. These findings were attributed to DCBQ transformation by photolysis and the hydrolysis effect was found to be negligible.
Źródło:: Acta Biochimica Polonica; 2011, 58, 4; 627-633
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 3.

Tytuł:: Comparison of properties of amylophosphoric acid and di-starch phosphate salts
Autorzy:: Fortuna, T.
Gibinski, M.
Palasinski, M.
Powiązania:: https://bibliotekanauki.pl/articles/1371451.pdf
Data publikacji:: 1992
Wydawca:: Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Tematy:: calcium
physicochemical property
water binding capacity
sodium
paste transparency
di-starch phosphate salt
potassium
reducing capacity
salt
pasting
amylophosphoric acid salt
Źródło:: Polish Journal of Food and Nutrition Sciences; 1992, 01, 4; 115-120
1230-0322
2083-6007
Pojawia się w:: Polish Journal of Food and Nutrition Sciences
Dostawca treści:: Biblioteka Nauki

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