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tyrosinase/krumpir
Veza se sprema u međuspremnik
Stranica 1 iz 28 rezultatima
Electrochemical biosensor made with tyrosinase immobilized in a matrix of nanodiamonds and potato starch for detecting phenolic compounds.
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The envisaged ubiquitous sensing and biosensing for varied applications has motivated materials development toward low cost, biocompatible platforms. In this paper, we demonstrate that carbon nanodiamonds (NDs) can be combined with potato starch (PS) and be deposited on a glassy carbon electrode
Oil-in-water emulsions stabilized by tyrosinase-crosslinked potato protein.
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Potato protein (PP) holds great promise as a non-allergenic food ingredient with high nutritional value. Attempts to modulate its functional properties by crosslinking have not been reported to date. The effect of tyrosinase-mediated crosslinking of PP on the properties of o/w emulsions was studied
[On the ability of monophenols to submit to o-hydroxylation and to serve as coenzymes in the oxidation of ascorbic acid in the presence of potato tyrosinase].
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[Quantitative determination of phenoloxidase (EC 1.14.18.1). Absorption behavior of mushroom and potato tyrosinase].
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[ON THE COUPLED OXIDATION OF 1,4-BENZENEDIOL AND ASCORBIC ACID BY POTATO TYROSINASE. MECHANISM OF THE REACTION].
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ENZYMATIC OXIDATION OF DIHYDROTHIAMINE. I. OXIDATION BY POTATO TYROSINASE.
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[Activation by triton X-100 of tyrosinases of potato sections].
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[Quantitative determination of phenoloxidase (EC 1.14.18.1). Spectrophotometry measurement of the activity of mushroom and potato tyrosinase].
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With dopa as substrat the enzyme were incubated 20 min in 0.1 M phosphate buffer, pH 6.8. After that the activity was detected at wavelengths of 313 and 492 nm using a layer thickness of 10 mm. Employing this conditions higher activities were estimated in the commercial preparates as indicated. The
The Action of Potato-tyrosinase on Adrenalin.
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Inhibition of potato polyphenol oxidase by anions and activity in various carboxylate buffers (pH 4.8) at constant ionic strength.
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The activity of potato polyphenol oxidase (tyrosinase) toward DL-3,4-dihydroxyphenylalanine (K(M) 5.39 mM) was studied using a variety of carboxylate buffers at a common pH and ionic strength. Enzyme activity, greatest in citrate and least in oxalate, correlated with increasing carboxyl
New potent inhibitors of tyrosinase: novel clues to binding of 1,3,4-thiadiazole-2(3H)-thiones, 1,3,4-oxadiazole-2(3H)-thiones, 4-amino-1,2,4-triazole-5(4H)-thiones, and substituted hydrazides to the dicopper active site.
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A series of 1,3,4-thiadiazole-2(3H)-thiones, 1,3,4-oxadiazole-2(3H)-thiones, 4-amino-1,2,4-triazole-5(4H)-thiones, and substituted hydrazides were tailored and synthesized as new potent inhibitors of tyrosinase. The rationale for inhibitor design was based on the active site structural evidence from
TYROSINASE AND PLANT RESPIRATION.
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The evidence presented in this paper supports the conclusion that at least 85 per cent of the oxygen uptake of the respiring tissue of potato tuber enters the chemistry of the cell by way of a tyrosinase-catalyzed oxidation. The qualitative aspects of this conclusion are in agreement with the claim
Degradation of tyrosinase induced by phenylthiourea occurs following Golgi maturation.
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Tyrosinase, the rate-limiting enzyme of melanin synthesis, is a di-copper metalloprotein that catalyzes the conversion of L-tyrosine to L-DOPAquinone. Phenylthiourea (PTU) is a well-known inhibitor of tyrosinase and melanin synthesis and is known to interact with sweet potato catechol oxidase, an
Flow injection spectrophotometric determination of L-Dopa and carbidopa in pharmaceutical formulations using a crude extract of sweet potato root [Ipomoea batatas (L.) Lam.] as enzymatic source.
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A flow injection (FI) spectrophotometric method is proposed for the determination of L-dopa and carbidopa in pharmaceutical formulations. After selection of the extraction medium (e.g., buffer-to-tissue ratio, pH, buffer concentration, protective agents and/or stabilizers) and storage conditions,
cDNA cloning and expression of potato polyphenol oxidase.
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Polyphenol oxidases (PPOs) of plants are copper metalloproteins which catalyze the oxidation of mono- and o-diphenols to o-diquinones. Although PPOs are believed to be primarily responsible for the deleterious browning of many fruit and vegetable crops and are thought to be involved in plant-pest
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