Detailed Mode of Action of Arabinan-Debranching ��-L-Arabinofuranosidase GH51 from Bacillus velezensis

Oh, Gyo Won; Kang, Yewon; Choi, Chang-Yun; Kang, Soyoung; Kang, Jung-Hyun; Lee, Min-Jae Lee; Han, Nam Soo; Kim, Tae-Jip

doi:10.4014/jmb.1811.11035

Cited by 3 publications

(3 citation statements)

References 26 publications

(35 reference statements)

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“…The group of ABFs GH51 showing 23.9~25.9% amino acid sequence identity possess unique debranching activities on α-(1,2)- and/or α-(1,3)-L-arabinofuranosidic linkages, but not on α-(1,5)- linkages. Bacillus velezensis ABF can specifically hydrolyze α-(1,2)- and/or α-(1,3)-branches of sugar beet arabinan, BAOS, and AXOS, but it showed much lower activity towards α-(1,5)-linkages of short-chain LAOS [ 25 ]. Similar debranching modes of action were also reported on the other bacterial ABFs from Bacillus subtilis [ 11 ], Pseudomonas cellulosa [ 26 ], and Thermobacillus xylanilyticus [ 27 ].…”

Section: Resultsmentioning

confidence: 99%

Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera

Park

Choi

Kim

et al. 2021

J. Microbiol. Biotechnol.

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IntroductionL-Arabinose is a pentose sugar that can be obtained by the hydrolysis of various plant cell wall hemicellulosic polymers such as arabinoxylans and arabinans [1]. Due to the health-beneficial functions, L-arabinose and arabino-oligosaccharides (AOS) have been considered as promising candidates for low-calorie sweeteners and prebiotic materials [2][3][4]. For the enzymatic production of L-arabinose, α-L-arabinofuranosidase (ABF; E.C. 3.2.1.55) is the key player which catalyzes the exo-type hydrolysis of L-arabinose-containing polymers [5,6]. Especially, its synergistic actions with endo-α-(1,5)-L-arabinanase (ABN; E.C. 3.2.1.99) were suggested for the cost-effective L-arabinose production from sugar beet arabinan [7,8].The ABFs possess versatile hydrolyzing activities towards the terminal non-reducing α-(1,2)-, α-(1,3)-, and/or α-(1,5)-L-arabinofuranosidic linkages in various polymeric and oligomeric substrates [5,6]. Depending on their structural features, the common microbial ABFs can be mainly categorized to the members of glycoside hydrolase (GH) families 51 and 43. To date, various ABFs have been reported from mainly bacteria, as well as a few fungi and plants [5,6,9]. Based on the genome analyses, the probable gene clusters for the utilization of L-arabinose and arabinans were found from Bacillus [10, 11], Geobacillus [12], and Corynebacterium spp. [13]. Bacillus subtilis produces two intracellular exo-ABFs GH51 and two extracellular endo-ABNs GH43, which can synergistically degrade the arabinan polymers to L-arabinose [11]. On the contrary, only a limited number of eukaryotic ABFs were genetically and enzymatically characterized from the fungal microorganisms such as Penicillium [14], Aspergillus [15], Chrysosporium [16], and Aureobasidium spp. [17]. As the eukaryotic ABFs share relatively low Two genes encoding probable α-L-arabinofuranosidase (E.C. 3.2.1.55) isozymes (ABFs) with 92.3% amino acid sequence identity, ABF51A and ABF51B, were found from chromosomes 3 and 5 of Saccharomycopsis fibuligera KJJ81, an amylolytic yeast isolated from Korean wheat-based nuruk, respectively. Each open reading frame consists of 1,551 nucleotides and encodes a protein of 517 amino acids with the molecular mass of approximately 59 kDa. These isozymes share approximately 49% amino acid sequence identity with eukaryotic ABFs from filamentous fungi. The corresponding genes were cloned, functionally expressed, and purified from Escherichia coli. SfABF51 A and SfABF51 B showed the highest activities on p-nitrophenyl arabinofuranoside at 40~45 o C and pH 7.0 in sodium phosphate buffer and at 50 o C and pH 6.0 in sodium acetate buffer, respectively. These exoacting enzymes belonging to the glycoside hydrolase (GH) family 51 could hydrolyze arabinoxylooligosaccharides (AXOS) and arabino-oligosaccharides (AOS) to produce only L-arabinose, whereas they could hardly degrade any polymeric substrates including arabinans and arabinoxylans. The detailed product analyses revealed that both SfABF51 isozymes can catalyze the ver...

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Section: Resultsmentioning

confidence: 99%

Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera

Park

Choi

Kim

et al. 2021

J. Microbiol. Biotechnol.

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“…AFase activity throughout the purification procedure was determined using p-NPAF as the substrate (4 mM) according to the method of Oh et al [21]. The substrate solution (250 µL) was mixed with 100 mM sodium acetate buffer (pH 5.5, 500 µL), and then a diluted enzyme solution (250 µL) was added.…”

Section: Enzyme Activity Assaymentioning

confidence: 99%

A Glycoside Hydrolase Family 62 A-L-Arabinofuranosidase from Trichoderma Reesei and Its Applicable Potential during Mashing

Sun

Xu²,

Lü

2020

Foods

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Arabinoxylan is the second most abundant component in the endosperm cell wall of barley and it has been shown to have negative effects on the viscosity and filtration rate of wort and beer. In this study, a glycoside hydrolase (GH) family 62 α-L-arabinofuranosidase (AFase), termed as TrAbf62A, was purified from the culture filtrate of Trichoderma reesei CICC 41495 by a combined chromatographic method. The preferred substrates of the purified TrAbf62A were soluble, highly substituted arabinoxylan oligosaccharides and polymers, similar to the type found in barley grain. TrAbf62A exhibited activity towards oligomeric and polymeric arabinoxylans, as well as colorimetric arabinose-based substrates, thus meeting the criteria to be classified as a type B AFase. TrAbf62A released mainly arabinose and xylose from soluble wheat arabinoxylan, thus indicating a dual lytic enzyme activity. Supplementation of TrAbf62A during mashing, with a loading of 12 mU/g malt, resulted in a 36.3% decrease in arabinoxylan polymer content, a 5.6% reduction in viscosity, and finally, a 22.1% increase in filtration rate. These results revealed that TrAbf62A has a high potential value in improving lautering performance during mashing.

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“…These enzymes belong to the Glycoside Hydrolase (GH) 2, 3, 43, 51, 54, and 62 families [ , accessed on 10 January 2024], which catalyze the hydrolysis of terminal non-reducing α-1,2-, α-1,3-, and/or α-1,5-arabinofuranoside residues from AOS and arabinans. Most ABFs have been found in various bacteria, such as Cellvibrio [ 17 ], Streptomyces [ 18 ], Thermotoga [ 19 ], Lactobacillus [ 20 ], Bacillus [ 21 , 22 ], Caldicellulosiruptor [ 23 ], Geobacillus [ 24 ], Clostridium [ 25 ], Bifidobacterium [ 26 , 27 ], and Weissella [ 28 ] species and so on, as well as from fungi and yeasts [ 29 , 30 ]. Meanwhile, endo-α-1,5- l -arabinanases (ABNs; EC 3.2.1.99) belong to the GH43 family and specifically hydrolyze arabinans into short-chain AOS.…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster of Bifidobacterium longum subsp. suis

Kang,

Choi,

Kang

et al. 2024

IJMS

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Bifidobacteria are probiotic microorganisms commonly found in the gastrointestinal tract, some of which are known to utilize linear arabino-oligosaccharides (AOS) as prebiotic carbohydrates. In general, the synergistic actions of exo-type α-l-arabinofuranosidases (ABFs) and endo-α-1,5-l-arabinanases (ABNs) are required for efficient arabinan degradation. In this study, the putative gene cluster for arabinan degradation was discovered in the genome of Bifidobacterium longum subsp. suis. It consists of a variety of genes encoding exo- and endo-hydrolases, sugar-binding proteins, ABC-binding cassettes, and transcriptional regulators. Among them, two endo-ABNs GH43 (BflsABN43A and BflsABN43B), two exo-ABFs GH43 (BflsABF43A and BflsABF43B), and an exo-ABF GH51 (BflsABF51) were predicted to be the key hydrolases for arabinan degradation. These hydrolase genes were functionally expressed in Escherichia coli, and their enzymatic properties were characterized. Their synergism in arabinan degradation has been proposed from the detailed modes of action. Extracellular endo-BflsABN43A hydrolyzes sugar beet and debranched arabinans into the short-chain branched and linear AOS. Intracellularly, AOS can be further degraded into l-arabinose via the cooperative actions of endo-BflsABN43B, exo-BflsABF43A with debranching activity, α-1,5-linkage-specific exo-BflsABF43B, and exo-BflsABF51 with dual activities. The resulting l-arabinose is expected to be metabolized into energy through the pentose phosphate pathway by three enzymes expressed from the ara operon of bifidobacteria. It is anticipated that uncovering arabinan utilization gene clusters and their detailed functions in the genomes of diverse microorganisms will facilitate the development of customized synbiotics.

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Detailed Mode of Action of Arabinan-Debranching ��-L-Arabinofuranosidase GH51 from Bacillus velezensis

Cited by 3 publications

References 26 publications

Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera

Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera

A Glycoside Hydrolase Family 62 A-L-Arabinofuranosidase from Trichoderma Reesei and Its Applicable Potential during Mashing

Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster of Bifidobacterium longum subsp. suis

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