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Author: search.filters.author.Sornyotha, SomphitSubject: search.filters.subject.Xylanolytic enzyme

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    Chemical pretreatment-independent saccharifications of xylan and cellulose of rice straw by bacterial weak lignin-binding xylanolytic and cellulolytic enzymes
    (2017-11-01)
    Teeravivattanakit, Thitiporn
    ;
    Baramee, Sirilak
    ;
    Phitsuwan, Paripok
    ;
    Sornyotha, Somphit
    ;
    Waeonukul, Rattiya
    Complete utilization of carbohydrate fractions is one of the prerequisites for obtaining economically favorable lignocellulosic biomass conversion. This study shows that xylan in untreated rice straw was saccharified to xylose in one step without chemical pretreatment, yielding 58.2% of the theoretically maximum value by Paenibacillus curdlanolyticus B-6 PcAxy43A, a weak lignin-binding trifunctional xylanolytic enzyme, endoxylanase/β-xylosidase/arabinoxylan arabinofuranohydrolase. Moreover, xylose yield from untreated rice straw was enhanced to 78.9% by adding endoxylanases PcXyn10C and PcXyn11A from the same bacterium, resulting in improvement of cellulose accessibility to cellulolytic enzyme. After autoclaving the xylanolytic enzyme-treated rice straw, it was subjected to subsequent saccharification by a combination of the Clostridium thermocellum endoglucanase CtCel9R and Thermoanaerobacter brockii β-glucosidase TbCglT, yielding 88.5% of the maximum glucose yield, which was higher than the glucose yield obtained from ammoniatreated rice straw saccharification (59.6%). Moreover, this work presents a new environment-friendly xylanolytic enzyme pretreatment for beneficial hydrolysis of xylan in various agricultural residues, such as rice straw and corn hull. It not only could improve cellulose saccharification but also produced xylose, leading to an improvement of the overall fermentable sugar yields without chemical pretreatment.
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    Multifunctional properties of glycoside hydrolase family 43 from Paenibacillus curdlanolyticus strain B-6 including exo-β-xylosidase, endo-xylanase, and α-L-arabinofuranosidase activities
    (2015-01-01)
    Wongratpanya, Kanok
    ;
    Imjongjairak, Siriluck
    ;
    Waeonukul, Rattiya
    ;
    Sornyotha, Somphit
    ;
    Phitsuwan, Paripok
    The glycoside hydrolase family 43 from Paenibacillus curdlanolyticus strain B-6 (GH43B6) exhibited multifunctional properties, including exo-β-xylosidase, endo-xylanase, and α-L-arabinofuranosidase enzymatic activities. GH43B6 released xylose as a hydrolysis product from the successive reduction of xylooligosaccharides as a result of exo-β-xylosidase activity. Moreover, GH43B6 also predominantly released xylose from low-substituted xylan derived from birchwood. However, when the highly substituted rye flour arabinoxylan was used as a substrate, exo-β-xylosidase activity changed to endo-xylanase activity, indicating that the enzymatic property of GH43B6 is influenced by the substituted side groups of xylan. For α-L-arabinofuranosidase, arabinose was released from short-chain substrates including p-nitrophenyl-α-L-arabinofuranoside and α-L-Araf-(1→2)-[α-L-Araf-(1→3)]-β-D-Xylp. This study reports the novel trifunctional properties of GH43B6 containing exo- and endo-activity together with xylanolytic debranching enzymatic activity, which increases its potential for application in lignocellulose-based biorefineries.