Activity,origins and location of cellulases in a silt loam soil |
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Authors: | C F A Hope R G Burns |
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Institution: | (1) Biological Laboratory, University of Kent, CT2 7NJ Canterbury, Kent, UK;(2) Present address: Department of Microbiology, University of Surrey, GU2 5XH Guildford, Surrey, UK |
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Abstract: | Summary Cellulase activity in a silt loam soil was assayed and characterised using a microcrystalline cellulose substrate (Avicel). Activity was maximal between pH 5.3 and pH 6.0. A 64% loss in activity was observed on air-drying the soil. However, the residual activity was stable to storage at 40°C for 7 days and was resistant to the action of added protease. The component endoglucanase and -D-glucosidase activities in field-moist and air-dried soil were also assayed. The proportion of the soil microbial population able to utilise cellulose was investigated and the persistence of two free (soluble) cellulase preparations of microbial origin was determined following their addition to soil. A rapid decline in the endoglucanase activity of a Streptomyces sp. cellulase preparation was observed while 30% of the original activity of a Trichoderma viride cellulase preparation could still be detected after 20 days. From the data obtained in this study it appears that the major portion of the -D-glucosidase activity is bound to and protected by the soil colloids. By contrast, the major portion of the exo- and endoglucanase activity appears to be free in the soil solution, attached to the outer surfaces of cellulolytic microorganisms or associated in enzyme substrate complexes. The low residual activity measured in air-dried soil may owe its stability to an association with soil colloids or with recalcitrant cellulosic material present in soil. |
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Keywords: | Soil cellulase Enzyme characterisation -D-Glucosidase" target="_blank">gif" alt="beta" align="MIDDLE" BORDER="0">-D-Glucosidase Trichoderma viride Endoglucanase |
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