Partial purification and properties of an endo-1,3-β-d-glucanase from germinated rye |
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Authors: | GM Ballance DJ Manners |
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Institution: | Department of Brewing and Biological Sciences, Heriot - Watt University, Edinburgh EH1 1HX, U.K. |
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Abstract: | An endo-1,3-β-d-glucanase from germinated rye was purified 58-fold by ion exchange chromatography on DEAE- and CM-cellulose, and by gel filtration on Bio Gel P-60. The enzyme had pH optima of 5.0 with laminarin and 5.7 with carboxymethyl pachyman and was stable up to 45°. Bovine serum albumin and certain chlorides increased the activity at low concentrations of buffer. With laminarin, the enzyme had a Km of 0.25 mg/ml and the MW was estimated to be 24 300. Isoelectric focusing indicated that the endo-1,3-/gb-d-glucanase was a basic protein. The properties of the enzyme are compared with those from other higher plants. |
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Keywords: | Gramineae germinated rye |
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