Abstract
The aim of this chapter is to provide a brief overview of the properties of several enzymes, included in the classes oxidoreductases (tyrosinase and lipoxygenase) and hydrolases (esterase and phosphatase), that were isolated from ascocarps of the desert truffle Terfezia claveryi Chatin. T. claveryi tyrosinase catalyzes the oxidation of monophenols (monophenolase activity) and their subsequent oxidation to o-quinones (diphenolase activity). This enzyme is one of the few fully latent tyrosinases characterized to date. Lipoxygenase uses molecular oxygen in the oxidation of certain polyunsaturated fatty acids, thus initiating the biosynthesis of oxylipins. Substrate and product specificity of a lipoxygenase, purified to apparent homogeneity from T. claveryi ascocarps, is reported. An enzyme responsible for the hydrolysis of p-nitrophenyl esters was also detected. The results obtained with different assays lead us to conclude that the enzyme responsible for this activity was an esterase and not a lipase. Both acid and alkaline phosphatases were present in the crude extract of T. claveryi ascocarps, alkaline phosphatase being the main one. The clear color of T. claveryi ascocarps permitted the direct localization of several enzymatic activities (esterase, alkaline phosphatase, and tyrosinase) in situ after incubating T. claveryi sections with the appropriate substrate. The main methods used to partially purify and characterize these enzymes are briefly described.
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This work has been supported by projects BIO2010-22225-C02-01 and CGL2011-29816 (MINECO-FEDER) and Project 04541/GERM/06 (Fundación Séneca, Región de Murcia, Spain).
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Pérez-Gilabert, M., García-Carmona, F., Morte, A. (2014). Enzymes in Terfezia claveryi Ascocarps. In: Kagan-Zur, V., Roth-Bejerano, N., Sitrit, Y., Morte, A. (eds) Desert Truffles. Soil Biology, vol 38. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-40096-4_16
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