Maggot chymotrypsin I from Lucilia sericata is resistant to endogenous wound protease inhibitors

作者：Telford G; Brown A P; Kind A; English J S C; Pritchard D I^*

来源：British Journal of Dermatology, 2011, 164(1): 192-196.

DOI：10.1111/j.1365-2133.2010.10081.x

P>Background
A chymotrypsin found in the secretions of Lucilia sericata and manufactured as a recombinant enzyme degrades chronic wound eschar ex vivo.
Objectives
To characterize the inhibition profile of the L. sericata recombinant chymotrypsin I.
Methods
Activity of recombinant chymotrypsin I and its sensitivity to endogenous inhibitors were determined enzymatically using the fluorogenic substrate succinyl-alanyl-alanyl-prolyl-phenylalanyl-aminomethyl coumarin.
Results
We report the presence of high concentrations of two endogenous inhibitors, alpha 1-antichymotrypsin and alpha 1-antitrypsin, in wound eschar and a trace of a third, alpha 2-macroglobulin, with the potential to inhibit this debridement process. However, the addition of a soluble and inhibitor-containing extract of chronic wound eschar to chymotrypsin I did not affect activity of the enzyme, neither did the addition of purified native alpha 1-antichymotrypsin or alpha 1-antitrypsin, although chymotrypsin I was inhibited by alpha 2-macroglobulin. Conversely, the mammalian equivalent, alpha-chymotrypsin, was inhibited by the purified native alpha 1-antichymotrypsin, alpha 1-antitrypsin and alpha 2-macroglobulin and by the soluble extract of wound eschar.
Conclusions
The data suggest that the maggot-derived chymotrypsin I is biochemically distinct from human alpha-chymotrypsin and the lack of inhibition by wound eschar suggests a means by which chymotrypsin I activity survives within the wound to contribute towards debridement during maggot biotherapy.

• 出版日期2011-1