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Titolo:
Latent polyphenol oxidases from sage log (Metroxylon sagu): Partial purification, activation, and some properties
Autore:
Onsa, GH; bin Saari, N; Selamat, J; Bakar, J;
Indirizzi:
Univ Pertanian Malaysia, Fac Food Sci & Biotechnol, Dept Food Sci, Serdang43400, Selangor, Malaysia Univ Pertanian Malaysia Serdang Selangor Malaysia 43400 elangor, Malaysia
Titolo Testata:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
fascicolo: 10, volume: 48, anno: 2000,
pagine: 5041 - 5045
SICI:
0021-8561(200010)48:10<5041:LPOFSL>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; APPLE POLYPHENOLOXIDASE; TRITON X-114;
Keywords:
Metroxylon sagu; pith; latent polyphenol oxidase; extraction; partial purification; characterization;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: bin Saari, N Univ Pertanian Malaysia, Fac Food Sci & Biotechnol, Dept FoodSci, Serdang43400, Selangor, Malaysia Univ Pertanian Malaysia Serdang Selangor Malaysia 43400 ysia
Citazione:
G.H. Onsa et al., "Latent polyphenol oxidases from sage log (Metroxylon sagu): Partial purification, activation, and some properties", J AGR FOOD, 48(10), 2000, pp. 5041-5045

Abstract

Latent polyphenol oxidase (LPPO), an enzyme responsible for the browning reaction of sage starches during processing and storage, was investigated. The enzyme was effectively extracted and partially purified from the pith using combinations of nonionic detergents. With Triton X-114 and a temperature-induced phase partitioning method, the enzyme showed a recovery of 70% and purification of 4.1-fold. Native PAGE analysis of the partially purified LPPO revealed three. activity bands when stained with catechol and two bands with pyrogallol. The molecular masses of the enzymes were estimated by SDS-PAGE to be 37, 45, and 53 kDa. The enzyme showed optimum pH values of 4.5with 4-methylcatechol as a substrate and 7.5 with pyrogallol. The LPPO washighly reactive toward diphenols and triphenols. The activity of the enzyme was greatly enhanced in the presence of trypsin, SDS, ethanol, and linoleic acid.

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Documento generato il 05/12/20 alle ore 01:18:58