Abstract
An aminopeptidase with relatively higher specificity towards N-terminal Pro residue was purified to homogeneity from chicken intestine. Peptide Mass Finger printing studies identified the enzyme as Leukotriene A4 hydrolase (LTA4H). The molecular weight of the enzyme was found to be 66kDa. The enzyme exhibited optimum activity at pH 7.5 and 55°C and showed activation individually by albumin, deoxycholate and anions like SCN−, Cl−, Br− and I−. Unlike its mammalian counterpart, chicken intestinal LTA4H exhibited highest activity towards N-terminal Pro followed by Leu and Ala and least towards Arg. The aminopeptidase activity was completely inhibited by 1,10 phenanthroline and bestatin, while partially by EDTA and pefabloc. Potential of this enzyme for its use in debittering of protein hydrolysate is discussed.
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