Cloning, purification, and characterization of galactomannan-degrading enzymes from Myceliophthora thermophila |
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Authors: | G S Dotsenko M V Semenova O A Sinitsyna S W A Hinz J Wery I N Zorov E G Kondratieva A P Sinitsyn |
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Institution: | 1. Chemical Faculty, Lomonosov Moscow State University, 119991, Moscow, Russia 2. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33/2, 119071, Moscow, Russia 3. Dyadic Nederland BV, Nieuwe Kanaal 7s, 6709 PA, Wageningen, The Netherlands
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Abstract: | Genes of β-mannosidase 97 kDa, GH family 2 (bMann9), β-mannanase 48 kDa, GH family 5 (bMan2), and α-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-β-D-mannopyranoside, and the optimal pH and temperature are 5.3 and 40°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°C, respectively. aGal1 is active towards p-nitrophenyl-α-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°C, respectively. |
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