Forskningsartikel2012Vetenskapligt granskad
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.
Sammanfattning
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.
Nyckelord
Myceliophthora thermophila; beta-mannosidase; beta-mannanase; alpha-galactosidase; enzymatic hydrolysis
Publicerad i
Биохимия / Biochemistry
2012, Volym: 77, nummer: 11, sidor: 1303-1311
UKÄ forskningsämne
Biokemi och molekylärbiologi
Publikationens identifierare
DOI: https://doi.org/10.1134/S0006297912110090
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/84283