Abstract:
:Endo-beta-1,4-xylanase X-I is a major hydrolase produced by the aleurone tissue of germinating barley grain. It was previously reported that this cytosolic enzyme is synthesized as an inactive precursor which is proteolytically processed to active forms upon its programmed cell death dependent release. We here demonstrate, however, that the precursor form of X-I is an active enzyme. Purified recombinant precursor X-I was characterised with respect to its molecular weight, iso-electric point and temperature and pH activity and stability. Analysis of the hydrolysis products showed that it is an endo-acting enzyme which has the striking ability to release xylose from both polymeric xylan as well as from small xylo-oligosaccharides. The implications of these findings in relation to the putative role of the N-terminal propeptide as a carbohydrate binding module and the possible consequences for the way X-I fulfils its role in the germination process, are discussed.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Van Campenhout S,Pollet A,Bourgois TM,Rombouts S,Beaugrand J,Gebruers K,De Backer E,Courtin CM,Delcour JA,Volckaert Gdoi
10.1016/j.bbrc.2007.03.066subject
Has Abstractpub_date
2007-05-11 00:00:00pages
799-804issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(07)00535-9journal_volume
356pub_type
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