Abstract
Publisher Summary This chapter discusses the purification procedure of β-lactamase (Bacillus licheniformis). The most convenient and effective method of releasing cell bound β-lactamase appears to be the treatment of lysed cells with trypsin. However, exposure of B. licheniformis cells to the action of chymotrypsin, pronase, or an aqueous solution of butan-1-ol (4% v/v) also releases the greater part of the enzyme attached to the cells. It is found that membrane-bound β-lactamase may also be released by the action of sodium deoxycholate. Trypsin-released β-lactamase can be purified by a combination of ammonium sulfate fractionation and DEAE-cellulose chromatography. The use of affinity chromatography has been introduced for the small-scale purification of B. licheniformis β-lactamase.
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