TY - CHAP
T1 - Isolation, purification and partial characterization of laccase from ustilago maydis
AU - Desentis-Mendoza, R. M.
AU - Hernández-Sánchez, H.
AU - Jaramillo-Flores, M. E.
N1 - Publisher Copyright:
© 2008, Springer Science+Business Media, LLC.
PY - 2008
Y1 - 2008
N2 - Huitlacoche is a fungus that has been consumed in Mexico since prehispanic times. This Aztec name is given to the galls or tumors that form in corn cobs by the fungus scientifically known as Ustilago maydis. When infection takes place, a great mass of mycelium is formed in different zones in the corn plant. In the end, a great mass of black spores replaces the mycelium, and it is at this stage that the product is consumed as food (Valverde et al., 1995). Laccase (p-diphenol oxygen oxidoreductase, E. C. 1.10.3.2) catalyzes the oxidation of p-hydroxyphenols. Its activity depends on copper, oxidizes o- and p-dihydroxyphenols and compounds such as p-phenylendiamine and syringaldazine to color final products. Laccases differ from p-diphenol oxidases in their ability to hydroxylate monophenols (Walker, 1995; Palmieri et al., 1997). The objective of this work was to isolate, purify and partially characterize (biochemically and physico-chemically) the laccase from U. maydis.
AB - Huitlacoche is a fungus that has been consumed in Mexico since prehispanic times. This Aztec name is given to the galls or tumors that form in corn cobs by the fungus scientifically known as Ustilago maydis. When infection takes place, a great mass of mycelium is formed in different zones in the corn plant. In the end, a great mass of black spores replaces the mycelium, and it is at this stage that the product is consumed as food (Valverde et al., 1995). Laccase (p-diphenol oxygen oxidoreductase, E. C. 1.10.3.2) catalyzes the oxidation of p-hydroxyphenols. Its activity depends on copper, oxidizes o- and p-dihydroxyphenols and compounds such as p-phenylendiamine and syringaldazine to color final products. Laccases differ from p-diphenol oxidases in their ability to hydroxylate monophenols (Walker, 1995; Palmieri et al., 1997). The objective of this work was to isolate, purify and partially characterize (biochemically and physico-chemically) the laccase from U. maydis.
KW - Denaturation temperature
KW - Great mass
KW - Laccase activity
KW - Partial characterization
KW - Pleurotus ostreatus
UR - http://www.scopus.com/inward/record.url?scp=85060569865&partnerID=8YFLogxK
U2 - 10.1007/978-0-387-75430-7_27
DO - 10.1007/978-0-387-75430-7_27
M3 - Capítulo
AN - SCOPUS:85060569865
T3 - Food Engineering Series
SP - 375
EP - 381
BT - Food Engineering Series
PB - Springer
ER -