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A novel GH43 α-l-arabinofuranosidase of Penicillium chrysogenum that preferentially degrades single-substituted arabinosyl side chains in arabinan

Paper ID Volume ID Publish Year Pages File Format Full-Text
17209 42651 2014 7 PDF Available
Title
A novel GH43 α-l-arabinofuranosidase of Penicillium chrysogenum that preferentially degrades single-substituted arabinosyl side chains in arabinan
Abstract

•The fourth α-l-arabinofuranosidase was purified from Penicillium chrysogenum.•The enzyme preferentially hydrolyzed arabinosyl side chains in l-arabinan.•The enzyme belongs to glycoside hydrolase family 43.•Expression of the gene in P. chrysogenum was induced with pectic components.

We previously described three α-l-arabinofuranosidases (ABFs) secreted by Penicillium chrysogenum 31B. Here, we purified a fourth ABF, termed PcABF43A, from the culture filtrate. The molecular mass of the enzyme was estimated to be 31 kDa. PcABF43A had the highest activity at 35 °C and at around pH 5. The enzyme activity was strong on sugar beet l-arabinan but weak on debranched arabinan and arabinoxylan. Low molecular-mass substrates such as p-nitrophenyl α-l-arabinofuranoside, α-1,5-l-arabinooligosaccharides, and branched arabinotriose were highly resistant to the action of PcABF43A. 1H-NMR analysis revealed that PcABF43A hydrolyzed arabinosyl side chains linked to C-2 or C-3 of single-substituted arabinose residues in l-arabinan. Reports concerning enzymes specific for l-arabinan are quite limited. Pcabf43A cDNA encoding PcABF43A was isolated by in vitro cloning. The deduced amino acid sequence of the enzyme shows high similarities with the sequences of other fungal uncharacterized proteins. Semi-quantitative RT-PCR analysis indicated that the Pcabf43A gene was constitutively expressed in P. chrysogenum 31B at a low level, although the expression was induced with pectic components such as l-arabinose, l-rhamnose, and d-galacturonic acid. Analysis of enzymatic characteristics of PcABF43A, GH51 ABF (AFQ1), and GH54 ABF (AFS1) from P. chrysogenum suggested that PcABF43A and AFS1 function as debranching enzymes and AFQ1 plays a role of saccharification in the degradation of l-arabinan by this fungus.

Keywords
ABFs, α-l-arabinofuranosidases; RG-I, rhamnogalacturonan-I; PNP, p-nitrophenyl; GH, glycoside hydrolase; Ara2, arabinofuranobiose; Ara3, arabinofuranotriose; HPAEC, high-performance anion-exchange chromatography; LC/IT/TOF MS, liquid chromatography/ion-tr
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A novel GH43 α-l-arabinofuranosidase of Penicillium chrysogenum that preferentially degrades single-substituted arabinosyl side chains in arabinan
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volumes 58–59, 10 May 2014, Pages 80–86
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us