Abstract:
:We screened an Aspergillus tubingensis expression library constructed in the yeast Kluyveromyces lactis for xylogalacturonan-hydrolyzing activity in microwell plates by using a bicinchoninic acid assay. This assay detects reducing carbohydrate groups when they are released from a carbohydrate by enzymatic activity. Two K. lactis recombinants exhibiting xylogalacturonan-hydrolyzing activity were found among the 3,400 colonies tested. The cDNA insert of these recombinants encoded a 406-amino-acid protein, designated XghA, which was encoded by a single-copy gene, xghA. A multiple-sequence alignment revealed that XghA was similar to both polygalacturonases (PGs) and rhamnogalacturonases. A detailed examination of conserved regions in the sequences of these enzymes revealed that XghA resembled PGs more. High-performance liquid chromatography and matrix-assisted laser desorption ionization-time of flight mass spectrometry of the products of degradation of xylogalacturonan and saponified modified hairy regions of apple pectin by XghA demonstrated that this enzyme uses an endo type of mechanism. XghA activity appeared to be specific for a xylose-substituted galacturonic acid backbone.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
van der Vlugt-Bergmans CJ,Meeuwsen PJ,Voragen AG,van Ooyen AJdoi
10.1128/aem.66.1.36-41.2000keywords:
subject
Has Abstractpub_date
2000-01-01 00:00:00pages
36-41issue
1eissn
0099-2240issn
1098-5336journal_volume
66pub_type
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pub_type: 杂志文章
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journal_title:Applied and environmental microbiology
pub_type: 杂志文章
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journal_title:Applied and environmental microbiology
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1997-03-01 00:00:00