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pubmed-article:18689518pubmed:abstractTextThe apuB gene of Bifidobacterium breve UCC2003 was shown to encode an extracellular amylopullulanase. ApuB is composed of a distinct N-terminally located alpha-amylase-containing domain which hydrolyzes alpha-1,4-glucosidic linkages in starch and related polysaccharides and a C-terminally located pullulanase-containing domain which hydrolyzes alpha-1,6 linkages in pullulan, allowing the classification of this enzyme as a bifunctional class II pullulanase. A knockout mutation of the apuB gene in B. breve UCC2003 rendered the resulting mutant incapable of growth in medium containing starch, amylopectin, glycogen, or pullulan as the sole carbon and energy source, confirming the crucial physiological role of this gene in starch metabolism.lld:pubmed
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pubmed-article:18689518pubmed:articleTitleCharacterization of ApuB, an extracellular type II amylopullulanase from Bifidobacterium breve UCC2003.lld:pubmed
pubmed-article:18689518pubmed:affiliationDepartment of Microbiology, Alimentary Pharmabiotic Centre and National University of Ireland, Cork, Western Road, Cork, Ireland.lld:pubmed
pubmed-article:18689518pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18689518pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed