exopeptidase

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ex·o·pep·ti·dase

 (ĕk′sō-pĕp′tĭ-dās′, -dāz′)
n.
Any of a group of enzymes that catalyze the hydrolysis of single amino acids from the end of a polypeptide chain.

exopeptidase

(ˌɛksəʊˈpɛptɪˌdeɪz)
n
(Biochemistry) any proteolytic enzyme, such as erepsin, that acts on the terminal bonds in a peptide chain. Compare endopeptidase
References in periodicals archive ?
In the herbivorous Colorado potato beetle, the food protein hydrolysis is achieved by the initial participation of an aspartic peptidase, followed by serine, cysteine peptidases and later by exopeptidases (Brunelle et al.
These results showed that Alcalase which is an endopeptidases can produce higher amount of peptides with smallest molecular size compared to Flavourzyme which is an exopeptidases.
Exopeptidases, such as Flavorpro[TM] 937MDP can be used to control bitterness by removing these bitter-tasting peptides.
This avoids MS analysis and interpretation of extremely complex peptide mixtures that might otherwise result from degradation by the omnipresent exopeptidases.
Glutalytic contains both endopeptidases and exopeptidases to create the correct endopeptidase cleavage pattern near the long chain amino acids that need to be hydrolyzed by the exopeptidase, producing rapid degradation of gluten.
Non-proteasome proteases have been divided into exopeptidases and endopeptidases depending on the cleavage position of target proteins.
The exopeptidases act on short chain peptides that are produced by the action of endopeptidases, thus acting as polymer terminal enzymes as part of a cascade effect in protien catabolism.