Role of Two α-l-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori

Koseki, Takuya; Okuda, Masaki; Sudoh, Shigetoshi; Kizaki, Yasuzo; Iwano, Kimio; Aramaki, Isao; Matsuzawa, Hiroshi

doi:10.1016/s1389-1723(03)80187-1

Cited by 34 publications

(20 citation statements)

References 25 publications

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“…α-L-arabinofuranosidase catalyzes the hydrolysis of α-1,2-, α-1,2-, α-1,3-and α-1,5-L-arabinofuranosidic bonds in L-arabinose-containing hemicelluloses such as arabinoxylan and L-arabinan [29,30]. A. kawachii is an industrially important fungus in traditional Japanese liquor brewing and produces two different α-L-arabinofuranosidases, namely arabinofuranosidase A (AkAbfA) and arabinofuranosidase B (AkAbfB) [31]. AkAbfA and AkAbfB are assigned to families GH51 and GH54, respectively.…”

Section: Family 42 Cbm Structure Reveals a β-Trefoil Fold Related To mentioning

confidence: 99%

Recent structural studies of carbohydrate-binding modules

Hashimoto

2006

Cell. Mol. Life Sci.

161

123

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Carbohydrate-binding modules (CBMs) are found in many carbohydrate-active enzymes. CBMs bind to a range of polysaccharides, their primary function being to increase the catalytic efficiency of the carbohydrate-active enzymes against soluble and/or insoluble substrates. CBMs bind to their target ligands with high specificities and affinities. Thus, CBM systems are excellent models to study the mechanism of protein-carbohydrate interaction. To date, CBMs have been classified into 45 different families and many structural and functional studies have been reported. At present, three-dimensional structures of CBMs from 31 different families have been determined. These structures demonstrate that the fold most commonly found in CBMs is the beta-sandwich. In the past few years, about 10 new structures from different families have been reported. These enable detailed classification of CBM structures. This article reviews recent structural and functional studies of CBMs and discusses the sub-classification of beta-sandwich CBMs.

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Section: Family 42 Cbm Structure Reveals a β-Trefoil Fold Related To mentioning

confidence: 99%

Recent structural studies of carbohydrate-binding modules

Hashimoto

2006

Cell. Mol. Life Sci.

161

123

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“…However, other authors report the synergistic action of these enzymes with other pectinases and hemicellulases on lignocelluloses. For instance, the two enzymes a-L-AFases (kabfA and kabjB) from Aspergillus kawachii acted synergistically with xylanase in the degradation of arabinoxylan, releasing higher amounts of ferulic acid in the presence of feruloyl esterase [68]. Furthermore, Hashimoto and Nakata [51] showed that hemicellulose from soy sauce materials was decomposed synergistically by xylanase, b-xylosidase and a-L-AFase produced by Aspergillus oryzae HL15 during moromi 1 fermentation.…”

Section: The A-l-afasesmentioning

confidence: 99%

“…Generally, arabinose-containing substrates are essential for the efficient production of a-L-AFases [9,68]. Monomeric compounds L-arabitol and L-arabinose induce the genes involved in the production of these enzymes in some microorganisms [27].…”

Section: Production Of A-l-afasesmentioning

confidence: 99%

“…Monomeric compounds L-arabitol and L-arabinose induce the genes involved in the production of these enzymes in some microorganisms [27]. Conversely, other monosaccharides such as glucose and galactose may inhibit the production of a-L-AFases [9,68]. Arabinogalactans and oatmeal were found to be the best inducers for a-L-AFase isolated from Bacillus pumilus PS213 [32].…”

Section: Production Of A-l-afasesmentioning

confidence: 99%

“…a-L-AFase was produced by Rhodothermus marinus when the culture was grown on birchwood xylan [46]. L-Arabitol was the inducer for the production of a-L-AFases enzymes araA and araB by the A. niger mutants [26]; ABF1 by the Penicillium purpurogenum [15,27] and kabfA and kabjB by the A. kawachii [68]. a-L-AFase production by Pseudomona cellulosa was repressed when glucose was used in the production medium [9].…”

Section: Production Of A-l-afasesmentioning

confidence: 99%

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α-l-Arabinofuranosidases: the potential applications in biotechnology

Numan

Bhosle

2005

J IND MICROBIOL BIOTECHNOL

161

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Recently, alpha-L-arabinofuranosidases (EC3.2.1.55) have received increased attention primarily due to their role in the degradation of lignocelluloses as well as their positive effect on the activity of other enzymes acting on lignocelluloses. As a result, these enzymes are used in many biotechnological applications including wine industry, clarification of fruit juices, digestion enhancement of animal feedstuffs and as a natural improver for bread. Moreover, these enzymes could be used to improve existing technologies and to develop new technologies. The production, mechanisms of action, classification, synergistic role, biochemical properties, substrate specificities, molecular biology and biotechnological applications of these enzymes have been reviewed in this article.

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Feed Enzymes: Source and Applications

Singh

Yadav

2018

Enzymes in Food Technology

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Role of Two α-l-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori

Cited by 34 publications

References 25 publications

Recent structural studies of carbohydrate-binding modules

Recent structural studies of carbohydrate-binding modules

α-l-Arabinofuranosidases: the potential applications in biotechnology

Feed Enzymes: Source and Applications

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