Substrate Recognition of a Family 10 Xylanase from Streptomyces olivaceoviridis E-86: A Study by Site-directed Mutagenesis to Make an Hindrance around the Entrance toward the Substrate-binding Cleft

金子, 哲; 一ノ瀬, 仁美; 藤本, 瑞; 岩松, 新之輔; 久野, 敦; 長谷川, 典巳

doi:10.5458/jag.56.173

Cited by 7 publications

(4 citation statements)

References 36 publications

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“…One of the xylanases produced by S. olivaceoviridis E-86 is SoXyn10A (formerly FXYN), which is one of the most well-characterized xylanases. 15) 16) 17) The following functional properties of SoXyn10A have been studied in detail: sugar-binding structures with various kinds of xylooligosacchrides, 18) 19) mechanism of enzyme catalysis, 20) 21) 22) topology of the substrate binding cleft, 23) 24) protein engineering 25) 26) 27) and production of xylooligosaccharides. 28) 29) 30) 31) 32) In contrast, the other xylanase produced by S. olivaceoviridis E-86 designated as SoXyn11B (formerly GXYN) has not been well-characterized.…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of the GH10 and GH11 Xylanases from <i>Streptomyces olivaceoviridis</i> E-86 Provide Insights into the Advantage of GH11 Xylanase in Catalyzing Biomass Degradation

et al. 2019

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We functionally characterized the GH10 xylanase (SoXyn10A) and the GH11 xylanase (SoXyn11B) derived from the actinomycete Streptomyces olivaceoviridis E-86. Each enzyme exhibited differences in the produced reducing power upon degradation of xylan substrates. SoXyn10A produced higher reducing power than SoXyn11B. Gel filtration of the hydrolysates generated by both enzymes revealed that the original substrate was completely decomposed. Enzyme mixtures of SoXyn10A and SoXyn11B produced the same level of reducing power as SoXyn10A alone. These observations were in good agreement with the composition of the hydrolysis products. The hydrolysis products derived from the incubation of soluble birchwood xylan with a mixture of SoXyn10A and SoXyn11B produced the same products as SoXyn10A alone with similar compositions. Furthermore, the addition of SoXyn10A following SoXyn11B-mediated digestion of xylan produced the same products as SoXyn10A alone with similar compositions. Thus, it was hypothesized that SoXyn10A could degrade xylans to a smaller size than SoXyn11B. In contrast to the soluble xylans as the substrate, the produced reducing power generated by both enzymes was not significantly different when pretreated milled bagasses were used as substrates. Quantification of the pentose content in the milled bagasse residues after the enzyme digestions revealed that SoXyn11B hydrolyzed xylans in pretreated milled bagasses much more efficiently than SoXyn10A. These data suggested that the GH10 xylanases can degrade soluble xylans smaller than the GH11 xylanases. However, the GH11 xylanases may be more efficient at catalyzing xylan degradation in natural environments (e.g. biomass) where xylans interact with celluloses and lignins.

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Section: Introductionmentioning

confidence: 99%

Functional Characterization of the GH10 and GH11 Xylanases from <i>Streptomyces olivaceoviridis</i> E-86 Provide Insights into the Advantage of GH11 Xylanase in Catalyzing Biomass Degradation

et al. 2019

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“…In addition to our work on SoCBM13, we have studied the function and structure of the catalytic module by various approaches including mutagenesis, module shuffling, and structural analysis. [62][63][64][65][66] …”

Section: Cbm13 Of Streptomyces Olivaceoviridis -Xylanasementioning

confidence: 99%

Structure and Function of Carbohydrate-Binding Module Families 13 and 42 of Glycoside Hydrolases, Comprising a β-Trefoil Fold

Fujimoto

2013

Bioscience, Biotechnology, and Biochemistry

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“…In order to increase the possible use of hemicellulose, our group has been studying the enzymatic degradation of hemicellulose. 3) 4) 5) 6) 7) 8) 9) 10) 11) 12) 13) 14) Biomass pretreatment is required prior to its enzymatic degradation. However, pretreatment methods to optimize enzyme-mediated recovery of hemicellulose have not been studied.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Ammonia Pretreatment for Enzymatic Hydrolysis of Sugarcane Bagasse to Recover Xylooligosaccharides

et al. 2020

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Sugarcane bagasse is a useful biomass resource. In the present study, we examined the efficacy of ammonia pretreatment for selective release of hemicellulose from bagasse. Pretreatment of bagasse with aqueous ammonia resulted in significant loss of xylan. In contrast, pretreatment of bagasse with anhydrous ammonia resulted in almost no xylan loss. Aqueous ammonia or anhydrous ammoniapretreated bagasse was then subjected to enzymatic digestion with a xylanase from the glycoside hydrolase (GH) family 10 or a xylanase from the GH family 11. The hydrolysis rate of xylan in bagasse pretreated with aqueous ammonia was approximately 50 %. In contrast, in the anhydrous ammoniatreated bagasse, xylan hydrolysis was > 80 %. These results suggested that anhydrous ammonia pretreatment would be an effective method for preparation of sugarcane bagasse for enzymatic hydrolysis to recover xylooligosaccharides.

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Substrate Recognition of a Family 10 Xylanase from Streptomyces olivaceoviridis E-86: A Study by Site-directed Mutagenesis to Make an Hindrance around the Entrance toward the Substrate-binding Cleft

Cited by 7 publications

References 36 publications

Functional Characterization of the GH10 and GH11 Xylanases from <i>Streptomyces olivaceoviridis</i> E-86 Provide Insights into the Advantage of GH11 Xylanase in Catalyzing Biomass Degradation

Functional Characterization of the GH10 and GH11 Xylanases from <i>Streptomyces olivaceoviridis</i> E-86 Provide Insights into the Advantage of GH11 Xylanase in Catalyzing Biomass Degradation

Structure and Function of Carbohydrate-Binding Module Families 13 and 42 of Glycoside Hydrolases, Comprising a β-Trefoil Fold

Evaluation of Ammonia Pretreatment for Enzymatic Hydrolysis of Sugarcane Bagasse to Recover Xylooligosaccharides

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