1887

Abstract

The xylanase Xys1L from JM8 is known to be processed extracellularly, to produce a protein of 33·7 kDa, Xys1S, that retains catalytic activity but not its cellulose-binding capacity. This paper demonstrates that at least five serine proteases isolated from spp. have the ability to process the xylanase Xys1L. The genes of two of these extracellular serine proteases, denominated SpB and SpC, were cloned from 66 (a strain commonly used as a host for protein secretion), sequenced, and overexpressed in ; both purified proteases were able to process Xys1L . Three other previously reported purified serine proteases, SAM-P20, SAM-P26 and SAM-P45, also processed Xys1L . The involvement of serine proteases in xylanase processing-degradation was demonstrated by co-expression of the xylanase gene () and the gene encoding the serine protease inhibitor (SLPI) from . Co-expression prevented processing and degradation of Xys1L and resulted in a threefold increase in the xylanase activity present in the culture supernatant. SpB and SpC also have the capacity to process other secreted proteins such as p40, a cellulose-binding protein from JM8, but do not have any clear effect on other secreted proteins such as amylase (Amy) from and xylanase Xyl30 from .

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2003-07-01
2019-11-23
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