α-l-Arabinofuranosidase from Streptomyces sp. PC22: Purification, characterization and its synergistic action with xylanolytic enzymes in the degradation of xylan and agricultural residues

Raweesri, P.; Riangrungrojana, P.; Pinphanichakarn, Pairoh

doi:10.1016/j.biortech.2008.05.016

Cited by 57 publications

(40 citation statements)

References 35 publications

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“…Furthermore, we also showed that β-xylosidase from this strain acts cooperatively with other xylanolytic enzymes from Streptomyces sp. PC22 to efficiently hydrolyze agricultural residues simply prepared as milled particles with no requirement for prior pretreatment with either chemicals or steam explosion (21). Here we report the ability of Streptomyces sp.…”

Section: Introductionmentioning

confidence: 95%

Glucose(xylose) isomerase production by Streptomyces sp. CH7 grown on agricultural residues

Chanitnun¹,

Pinphanichakarn²

2012

Braz. J. Microbiol.

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Streptomyces sp. CH7 was found to efficiently produce glucose(xylose) isomerase when grown on either xylan or agricultural residues. This strain produced a glucose(xylose) isomerase activity of roughly 1.8 U/mg of protein when it was grown in medium containing 1% xylose as a carbon source. Maximal enzymatic activities of about 5 and 3 U/mg were obtained when 1% xylan and 2.5% corn husks were used, respectively.The enzyme was purified from a mycelial extract to 16-fold purity with only two consecutive column chromatography steps using Macro-prep DEAE and Sephacryl-300, respectively. The approximate molecular weight of the purified enzyme is 170 kDa, and it has four identical subunits of 43.

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Section: Introductionmentioning

confidence: 95%

Glucose(xylose) isomerase production by Streptomyces sp. CH7 grown on agricultural residues

Chanitnun¹,

Pinphanichakarn²

2012

Braz. J. Microbiol.

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“…In this report, we provide biochemical evidence on how R. albus 8 might harness its arsenal of glycoside hydrolases to degrade different xylans to monomeric sugars that can then be metabolized. The synergistic effects of different xylanolytic enzymes have been previously demonstrated (6,16,24). However, to our knowledge this is the first report in which, at least, all of the enzymes minimally required for degradation of a hemicellulose were assembled from the same organism.…”

Section: Discussionmentioning

confidence: 65%

Biochemical Analyses of Multiple Endoxylanases from the Rumen Bacterium Ruminococcus albus 8 and Their Synergistic Activities with Accessory Hemicellulose-Degrading Enzymes

Moon

Iakiviak

Bauer

et al. 2011

Appl Environ Microbiol

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Ruminococcus albus 8 is a ruminal bacterium capable of metabolizing hemicellulose and cellulose, the major components of the plant cell wall. The enzymes that allow this bacterium to capture energy from the two polysaccharides, therefore, have potential application in plant cell wall depolymerization, a process critical to biofuel production. For this purpose, a partial genome sequence of R. albus 8 was generated. The genomic data depicted a bacterium endowed with multiple forms of plant cell wall-degrading enzymes. The endoxylanases of R. albus 8 exhibited diverse modular architectures, including incorporation of a catalytic module, a carbohydrate binding module, and a carbohydrate esterase module in a single polypeptide. The accessory enzymes of xylan degradation were a ␤-xylosidase, an ␣-L-arabinofuranosidase, and an ␣-glucuronidase. We hypothesized that due to the chemical complexity of the hemicellulose encountered in the rumen, the bacterium uses multiple endoxylanases, with subtle differences in substrate specificities, to attack the substrate, while the accessory enzymes hydrolyze the products to simple sugars for metabolism. To test this hypothesis, the genes encoding the predicted endoxylanases were expressed, and the proteins were biochemically characterized either alone or in combination with accessory enzymes. The different endoxylanase families exhibited different patterns of product release, with the family 11 endoxylanases releasing more products in synergy with the accessory enzymes from the more complex substrates. Aside from the insights into hemicellulose degradation by R. albus 8, this report should enhance our knowledge on designing effective enzyme cocktails for release of fermentable sugars in the biofuel industry.

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“…strain AHT-1 and Streptomyces sp. strain PC22 (13,33). Moreover, except for wheat arabinoxylan, the other three xylans were degraded synergistically by the enzymes in all simultaneous combinations.…”

Section: Discussionmentioning

confidence: 92%

“…Some GH-43 ␣-Larabinofuranosidases have both ␣-L-arabinofuranosidase and ␤-xylosidase activities (8,9). In combination with xylanase, ␣-Larabinofuranosidase, as well as other xylanolytic enzymes, such as ␤-xylosidase, ␣-glucuronidase, acetyl xylan esterase, and feruloyl esterase, can act synergistically and facilitate the complete hydrolysis of various substrates (10)(11)(12)(13)(14).…”

mentioning

confidence: 99%

Distinct Actions by Paenibacillus sp. Strain E18 α- l -Arabinofuranosidases and Xylanase in Xylan Degradation

Shi

Xiao-yan

Meng

et al. 2013

Appl Environ Microbiol

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We cloned a Paenibacillus sp. strain E18 5.3-kb xylanolytic gene cluster that contains three open reading frames encoding two family 43 ␣-L-arabinofuranosidases (Abf43A and Abf43B) and one family 10 xylanase (XynBE18). The deduced amino acid sequences of Abf43A and Abf43B were at most 68% and 63% identical to those of two putative family 43 proteins from Clostridium sp. strain DL-VIII (EHI98634.1 and EHI98635.1), respectively, but were only 11% identical to each other. Recombinant Abf43A and Abf43B had similar activities at 45°C and pH 6.0 but varied in thermostabilities and substrate specificities. Abf43B was active against only 4-nitrophenyl ␣-L-arabinofuranoside, whereas Abf43A acted on 4-nitrophenyl ␣-L-arabinofuranoside, wheat arabinoxylan, 4-nitrophenyl ␣-D-xylopyranoside, and sugar beet arabinan. The sequential and combined effects on xylan degradation by XynBE18, Abf43A, and Abf43B were characterized. For beechwood, birchwood, and oat spelt xylans as the substrates, synergistic effects were found when XynBE18 and Abf43A or Abf43B were incubated together and when the substrates were first incubated with Abf43A or Abf43B and then with XynBE18. Further high-performance liquid chromatography (HPLC) analysis showed that the amounts of xylobiose and xylose increased sharply in the aforementioned reactions. For water-soluble wheat arabinoxylan as the substrate, Abf43A not only released arabinose but also had a synergistic effect with XynBE18. Synergy may arise as the result of removal of arabinose residues from xylans by ␣-L-arabinofuranosidases, which eliminates steric hindrance caused by the arabinose side chains and which allows xylanases to then degrade the xylan backbone, producing short xylooligosaccharides.

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α-l-Arabinofuranosidase from Streptomyces sp. PC22: Purification, characterization and its synergistic action with xylanolytic enzymes in the degradation of xylan and agricultural residues

Cited by 57 publications

References 35 publications

Glucose(xylose) isomerase production by Streptomyces sp. CH7 grown on agricultural residues

Glucose(xylose) isomerase production by Streptomyces sp. CH7 grown on agricultural residues

Biochemical Analyses of Multiple Endoxylanases from the Rumen Bacterium Ruminococcus albus 8 and Their Synergistic Activities with Accessory Hemicellulose-Degrading Enzymes

Distinct Actions by Paenibacillus sp. Strain E18 α- l -Arabinofuranosidases and Xylanase in Xylan Degradation

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