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Research article2012Peer reviewed

Cloning, purification, and characterization of galactomannan-degrading enzymes from Myceliophthora thermophila

Dotsenko, G. S.; Semenova, M. V.; Sinitsyna, O. A.; Hinz, S. W. A.; Wery, J.; Zorov, I. N.; Kondratieva, E. G.; Sinitsyn, A. P.

Abstract

Genes of beta-mannosidase 97 kDa, GH family 2 (bMann9), beta-mannanase 48 kDa, GH family 5 (bMan2), and alpha-galactosidase 60 kDa, GH family 27 (aGal1) encoding galactomannan-degrading glycoside hydrolases of Myceliophthora thermophila C1 were successfully cloned, and the recombinant enzymes were purified to homogeneity and characterized. bMann9 displays only exo-mannosidase activity, the K (m) and k (cat) values are 0.4 mM and 15 sec(-1) for p-nitrophenyl-beta-D-mannopyranoside, and the optimal pH and temperature are 5.3 and 40 degrees C, respectively. bMann2 is active towards galac-tomannans (GM) of various structures. The K (m) and k (cat) values are 1.3 mg/ml and 67 sec(-1) for GM carob, and the optimal pH and temperature are 5.2 and 69 degrees C, respectively. aGal1 is active towards p-nitrophenyl-alpha-D-galactopyranoside (PNPG) as well as GM of various structures. The K (m) and k (cat) values are 0.08 mM and 35 sec(-1) for PNPG, and the optimal pH and temperature are 5.0 and 60 degrees C, respectively.

Keywords

Myceliophthora thermophila; beta-mannosidase; beta-mannanase; alpha-galactosidase; enzymatic hydrolysis

Published in

Биохимия / Biochemistry
2012, Volume: 77, number: 11, pages: 1303-1311

    UKÄ Subject classification

    Biochemistry and Molecular Biology

    Publication identifier

    DOI: https://doi.org/10.1134/S0006297912110090

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/84283