“…This last enzyme, which belongs to the family of M17 leucine aminopeptidases (LAPs), has been studied in great detail, including several investigations to identify the roles of conserved residues that are not directly involved in catalysis, metal ion binding, and/or substrate binding [187][188][189]. The thermostability of the B. kaustophilus LAP could be further enhanced by immobilization in Ca-alginate/k-carrageenan beads (ID 1270), whereas its resistance against oxidative damage was improved by replacement of the critical methionine residues with leucine [190]. This engineering study resulted in the generation of more active mutants as well.…”