Identification and characterization of three Penicillium chrysogenum α-l-arabinofuranosidases (PcABF43B, PcABF51C, and AFQ1) with different specificities toward arabino-oligosaccharides

Shinozaki, Ayaka; Hosokawa, Sachiko; Nakazawa, Masami; Ueda, Mitsuhiro; Sakamoto, Tatsuji

doi:10.1016/j.enzmictec.2015.04.003

Cited by 15 publications

(9 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As determined using the ProtParam tool, the theoretical MW and p I were 67.8 kDa and 5.71 for TtABF51A, or 32.8 kDa and 5.89 for EpABF62C. TtABF51A has its greatest homology to an uncharacterized GH51 protein (GenBank XP_003658814.4) from Thermothelomyces thermophilus with approximately 71% identity and shares 53% identity with a characterized GH51 ABF (GenBank BAG71680.1) from Penicillium chrysogenum (Sakamoto et al 2013 ; Shinozaki et al 2015 ). EpABF62C showed 73% identity with a characterized ABF (GenBank CAA16189) belonging to GH62 from the bacterium Streptomyces coelicolor (Maehara et al 2014 ).…”

Section: Resultsmentioning

confidence: 99%

“…Compared with the individual enzymes, the total amount of released sugar from wheat arabinoxylan was increased to 2.92-fold with simultaneous addition of a GH51 ABF and the GH10 endoxylanase XynBE18 (Yang et al 2015 ). Currently, diverse ABFs from both fungal and bacterial sources have been reported, which may provide important information for the understanding of the enzymes (Amore et al 2012 ; Bouraoui et al 2016 ; Hu et al 2018 ; Kaur et al 2015 ; Shinozaki et al 2015 ; Wilkens et al 2017 ; Yang et al 2015 ).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization and functional analysis of two novel thermotolerant α-l-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum

Long

Sun

Lin

et al. 2020

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Arabinofuranose substitutions on xylan are known to interfere with enzymatic hydrolysis of this primary hemicellulose. In this work, two novel α-l-arabinofuranosidases (ABFs), TtABF51A from Thielavia terrestris and EpABF62C from Eupenicillium parvum, were characterized and functionally analyzed. From sequences analyses, TtABF51A and EpABF62C belong to glycoside hydrolase (GH) families 51 and 62, respectively. Recombinant TtABF51A showed high activity on 4-nitrophenyl-α-l-arabinofuranoside (83.39 U/mg), low-viscosity wheat arabinoxylan (WAX, 39.66 U/mg), high-viscosity rye arabinoxylan (RAX, 32.24 U/mg), and sugarbeet arabinan (25.69 U/mg), while EpABF62C preferred to degrade arabinoxylan. For EpABF62C, the rate of hydrolysis of RAX (94.10 U/mg) was 2.1 times that of WAX (45.46 U/mg). The optimal pH and reaction temperature for the two enzymes was between 4.0 and 4.5 and 65 °C, respectively. Calcium played an important role in the thermal stability of EpABF62C. TtABF51A and EpABF62C showed the highest thermal stabilities at pH 4.5 or 5.0, respectively. At their optimal pHs, TtABF51A and EpABF62C retained greater than 80% of their initial activities after incubation at 55 °C for 96 h or 144 h, respectively. 1H NMR analysis indicated that the two enzymes selectively removed arabinose linked to C-3 of mono-substituted xylose residues in WAX. Compared with the singular application of the GH10 xylanase EpXYN1 from E. parvum, co-digestions of WAX including TtABF51A and/or EpABF62C released 2.49, 3.38, and 4.81 times xylose or 3.38, 1.65, and 2.57 times of xylobiose, respectively. Meanwhile, the amount of arabinose released from WAX by TtABF51A with EpXYN1 was 2.11 times the amount with TtABF51A alone. Key points • Two novel α-l-arabinofuranosidases (ABFs) displayed high thermal stability. • The thermal stability of GH62 family EpABF62C was dependent on calcium. • Buffer pH affects the thermal stability of the two ABFs. • Both ABFs enhance the hydrolysis of WAX by a GH10 xylanase.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization and functional analysis of two novel thermotolerant α-l-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum

Long

Sun

Lin

et al. 2020

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…The first group releases L-arabinosyl residues from arabinooligosaccharides [6]. Interestingly, the AFase PcABF43B from Penicillium chrysogenum preferentially hydrolyzes arabinosidic side chains in branched arabino-oligosaccharides [7], so PcABF43B could be classified into the subtype of this group. The second group degrades L-arabinosidic linkages both on arabino-oligosaccharides and branched arabinans [8].…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of GH62 bacterial α-l-arabinofuranosidase from thermotolerant Streptomyces sp. SWU10 that preferentially degrades branched l-arabinofuranoses in wheat arabinoxylan

Phuengmaung

Kunishige

Sukhumsirichart

et al. 2018

Enzyme and Microbial Technology

Self Cite

View full text Add to dashboard Cite

We previously described thermotolerant Streptomyces sp. SWU10, which produced four endo-xylanases and one xylosidase able to digest xylan backbones. To achieve arabinoxylan degradation, the swu62A gene was cloned and overexpressed in Escherichia coli, and the recombinant enzyme, termed SWUAbf62A, was characterized. The 438 amino acids of SWUAbf62A revealed Glyco_hydro_62 and closely related with putative α-l-arabinofuranosidases belonging to glycoside hydrolase family 62. SWUAbf62A was purified in two steps, Ni-affinity and size-exclusion column chromatographies, and its molecular mass without signal peptide was determined to be 49 kDa. SWUAbf62A showed optimum activity at pH 5.0 and 50 °C, and more than 70% of its initial enzymatic activity remained after incubation at pH 4.1-10.5, while SWUAbf62A lost all activity after 1 h at 60 °C. SWUAbf62A activity was stimulated by Ba, Ca, and Mn and decreased by Ag, Cu, Fe, and EDTA. SWUAbf62A had no activity towards p-nitrophenyl-α-l-arabinofuranoside or p-nitrophenyl-β-d-xylopyranoside synthetic substrates. On the other hand, SWUAbf62A had the highest activity against wheat arabinoxylan, with a specific activity of 1.29 U/mg, and was also active against sugar beet arabinan, with a specific activity of 0.14 U/mg; these results indicated that SWUAbf62A is an arabinoxylan arabinofuranohydrolase. Using H-NMR analysis, SWUAbf62A was found to release l-arabinofuranoses singly linked to O-3 of wheat arabinoxylan. In addition, SWUAbf62A acted synergistically with endo-xylanase (XynSW3) and α-l-arabinofuranosidase, which releases arabinose linked to O-3 of double-substituted xylose residues on arabinoxylan, to digest the wheat arabinoxylan. SWUAbf62A is an important debranching enzyme for hydrolysis of hemicelluloses to monosaccharides and can be applied in various industrial biotechnologies.

show abstract

“…They can be used as carbon sources in industrial fermentations producing antibiotics, industrial enzymes, and bulk chemicals, including ethanol. For these purposes, however, the polysaccharides in the biomass must first be hydrolyzed (Gottschalk et al, 2010;Shinozaki et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

“…3.1.1.72) and a-L-arabinofuranosidase (E.C. 3.2.1.55), which are able to release α-L-1,2-, α-L-1,3-and α-L-1,5-arabinofuranosyl side chains of arabinoxylans, arabinans and arabinogalactans (Temer et al, 2014;Shinozaki et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Trichoderma atroviride 102C1: A promising mutant strain for the production of a -glucosidase, -xylosidase and -L-arabinofuranosidase activities using agroindustrial by-products

Silva¹,

Grigorevski-Lima²,

Bon³

et al. 2018

Afr. J. Biotechnol.

View full text Add to dashboard Cite

Holocellulolytic accessory enzymes are very important in assisting hydrolysis of biomass. The use of these enzymes in the enzymatic hydrolysis of plant biomass is very important for obtaining building blocks in the concept of biorefinery. In previous studies, the mutant strain Trichoderma atroviride 102C1 was tested for production of endoglucanases, FPases and endoxylanases. This study aimed at evaluating the efficiency in holocellulolytic accessories enzymes production (-glucosidase, xylosidase and -L-arabinofuranosidase) by Trichoderma atroviride 102C1 using different lignocelluloses biomass as substrates. Accessory enzymes production was carried out in Erlenmeyer flasks containing Mandels salt medium, supplemented with different concentrations of sugarcane bagasse (SCB) and corn steep liquor (CSL), according to a Central Composite Rotational Design (CCRD). The fermentation system was incubated under agitation for 2 days / 28°C. For pH and temperature profile studies, a new CCRD was carried out. The best condition common to all enzymes, 55.4 U.mL-1 (β-glucosidase), 10.8 U.mL-1 (β-xylosidase) and 143.23 U.mL-1 (α-L-arabinofuranosidase), was observed when 2.5% (w/v) sugarcane bagasse (SCB) and 1.26% (w/v) of corn steep liquor (CSL) were used. All enzymes presented acidophilic characteristic in two different temperatures (44 and 55°C). The optimal profile characteristic for β-glucosidase and β-xylosidase activities were pH 5.0 and 3.0, respectively, both at 55°C, while for α-L-arabinofuranosidase it was pH 3.6 at 44°C. This study demonstrated the potential of T. atroviride 102C1 to produce three important holocellulolytic accessory enzymes in the presence of SCB and CSL, suggesting its use for enzymatic hydrolysis of lignocellulosic biomass.

show abstract

Identification and characterization of three Penicillium chrysogenum α-l-arabinofuranosidases (PcABF43B, PcABF51C, and AFQ1) with different specificities toward arabino-oligosaccharides

Cited by 15 publications

References 37 publications

Characterization and functional analysis of two novel thermotolerant α-l-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum

Characterization and functional analysis of two novel thermotolerant α-l-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum

Identification and characterization of GH62 bacterial α-l-arabinofuranosidase from thermotolerant Streptomyces sp. SWU10 that preferentially degrades branched l-arabinofuranoses in wheat arabinoxylan

Trichoderma atroviride 102C1: A promising mutant strain for the production of a -glucosidase, -xylosidase and -L-arabinofuranosidase activities using agroindustrial by-products

Contact Info

Product

Resources

About