Abstract

This chapter focuses on Lysine fermentation (Clostridium). The fermentation of lysine to fatty acids and ammonia by Clostridium sticklandii and certain other unidentified clostridial strains such as Clostridium M-E and Clostridium SB4 is a complex series of reactions. Growing cultures and suspensions of intact cells effect two types of cleavage of the carbon skeleton of lysine. In addition to the enzymes specific for L-α-lysine and D-α-lysine, a powerful racemase that interconverts these isomers is present in extracts of C. sticklandii and CIostridium M-E. The various diaminohexanoates that are interconverted in the lysine fermentation can be detected by a combination of chromatographic and electrophoretic procedures. When subjected to high voltage electrophoresis on Whatman 3 MM paper at pH 3.5, the basic amino acids migrate the following distances from the origin toward the cathode (cm): 3,6-diaminohexanoate (β-1ysine), 58.5; 3,5-diaminohexanoate, 53.5; and 2,6-diaminohexanoate (α-lysine), 49.5. At this pH, 2,5-diaminohexanoate has virtually the same mobility as α-lysine.

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