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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Fig. 2

Temperature dependence for TatCel7A_CD, ThaCel7A_CD, and TreCel7A_CD activity on pNP-Lac. a Temperature optimum for 1 h of hydrolysis at indicated temperatures. b Temperature stability of TreCel7A_CD. c Temperature stability of TatCel7A_CD. d Temperature stability of ThaCel7A_CD. For bd the enzymes were pre-incubated at 60, 65 and 70 °C at pH 4.5. At indicated time points, samples were cooled on ice followed by determination of residual activity at 30 °C. All reactions in ad contained 0.15 µM enzyme and 2 mM pNP-Lac and were incubated for 1 h at pH 4.5. Thereafter, the increase in pNP concentration was measured and divided by the incubation time (60 min) to yield the hydrolysis rates plotted on the y-axis. Error bars indicate the standard deviation of triplicate measurements

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