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- W1784292502 abstract "This chapter describes the engineering of the thermotolerance and pH optimum of family 11 xylanases by site-directed mutagenesis. The potential of using xylanases in industrial applications generated an intensive academic and industrial activity to hunt xylanases with desired properties from all kinds of natural sources. The thermostability of mesophilic xylanases has been increased considerably by designed mutations. T. reesei xylanase II (XYNII) is stable at 40–45°C, whereas temperatures above 50°C cause conformational changes and the enzyme activity is lost quite quickly. A combination of various mutations has often a cumulative effect on the thermostability of family 11 xylanases. It is observed that when mutations with only a small stabilizing effect were combined with the disulfide bridge engineered into α helix, a considerable increase in thermostability was achieved. It is found that xylanase activity is determined by using the 3,5-dinitrosalicylic acid assay to measure the amount of reducing sugars liberated from 1% birchwood xylan." @default.
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- W1784292502 date "2004-01-01" @default.
- W1784292502 modified "2023-10-16" @default.
- W1784292502 title "Engineering the Thermotolerance and pH Optimum of Family 11 Xylanases by Site-Directed Mutagenesis" @default.
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- W1784292502 doi "https://doi.org/10.1016/s0076-6879(04)88014-5" @default.
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