EFFECT OF AMINO ACIDS AND ALDEHYDES ON TYROSINASE ACTIVITY FROM MARROW | ||||
| Journal of Plant Production | ||||
| Article 9, Volume 5, Issue 2, February 2014, Page 295-303 PDF (643.38 K) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/jpp.2014.53642 | ||||
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| Authors | ||||
| H. M. El-Shora; Rania M. Hegazy | ||||
| Botany Department, Faculty of Science, Mansoura University | ||||
| Abstract | ||||
| Tyrosinase (monophenol, O-diphenol: oxygen oxidoreductase, EC 1.14.18.1) is a copper-containing protein widely distributed in animals, plants and microorganisms. The enzyme was extracted from Cucurbitapepovar. cylindrica, (marrow, family:Cucurbitaceae). Proline, tryptophane, aspartic acid, cysteine, histidine, glycine, β-alanine and valinewere assayed for their effect on tyrosinase activity in different concentrations (2.5, 5, 7.5, 10 and 12.5 mM)in vitro. Histidine, aspartic acid, glycine and β-alanine induced tyrosinase activity gradually from 2.5 to 10 mM after which there was a decline in the enzyme activity. Tryptophane, valine and cysteine induced the activity up to 5 mM, while proline induced the activity from 2.5 to 7.5mM. Also, tyrosinase activity was assayed in presence of benzaldehyde, anisaldehyde (P-methoxybenzaldehyde) and acetaldehyde (0.1, 0.2, 0.3, 0.4 and 0.5 mM).It was found that the enzyme activity was inhibited by the three tested aldehydes. | ||||
| Keywords | ||||
| Tyrosinase; Tyrosine; Amino acids; Benzaldehyde; Anisaldehyde; Acetaldehyde | ||||
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