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Characterization of a Thermostable and Acidic‐Tolerable β‐Glucanase from Aerobic Fungi Trichoderma koningii ZJU‐T
Author(s) -
Wang J.L.,
Ruan H.,
Zhang H.F.,
Zhang Q.,
Zhang H.B.,
He G.Q.,
Shen S.R.
Publication year - 2007
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2007.00549.x
Subject(s) - glucanase , chemistry , sodium , trichoderma , enzyme , biochemistry , food science , biology , horticulture , organic chemistry
An extreme thermostable and acidic tolerable β‐glucanase was isolated and characterized from aerobic fungi Trichoderma koningii ZJU‐T. The optimal reaction temperature and pH for the β‐glucanase were 100 °C and pH 2.0, respectively. The β‐glucanase showed increased stability at higher temperatures and lower pH values when compared to other β‐glucanases. The optimum conditions for the β‐glucanase stability were found to be pH 4.0 and 80 °C. Even subjected to 100 °C for 3 h, β‐glucanase activity did not show significant reduction. Moreover, K + significantly enhanced β‐glucanase activity at the concentration of 1 mM, while EDTA and other metal ions such as Mg 2+ , Mn 2+ , Zn 2+ , Ca 2+ , Fe 2+ , Pb 2+ , and Fe 3+ inhibited β‐glucanase activity. Denaturants, including sodium dodecyl sulfate (SDS) and mercaptoethanol, also inhibited β‐glucanase activity at a concentration of 5%. However, in the presence of 7 M urea, residual activity of the β‐glucanase still remained 14.5%.