Novel Alkali-Tolerant GH10 Endo-β-1,4-Xylanase with Broad Substrate Specificity from Microbacterium trichothecenolyticum HY-17, a Gut Bacterium of the Mole Cricket Gryllotalpa orientalis
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The XylH gene (1,167-bp) encoding a novel hemicellulase (41,584 Da) was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis. The enzyme consisted of a single catalytic domain, which is 74% identical to that of an endo-β-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-β- 1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multifunctional enzyme possessing endo-β-1,4-xylanase activity together with β-1,3/β-1,4- glucanase activity, which exhibited its highest xylanolytic activity at pH 9.0 and 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylosebased polysaccharides to the XylH were assessed to be as follows: oat spelts xylan > beechwood xylan > birchwood xylan > wheat arabinoxylan. rXylH was also able to readily cleave p-nitrophenyl (pNP) cellobioside and pNP-xylopyranoside, but did not hydrolyze other pNP-sugar derivatives, xylobiose, or hexose-based materials. Enzymatic hydrolysis of birchwood xylan resulted in the product composition of xylobiose (71.2%) and xylotriose (28.8%) as end products.
Abstract
The XylH gene (1,167-bp) encoding a novel hemicellulase (41,584 Da) was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis. The enzyme consisted of a single catalytic domain, which is 74% identical to that of an endo-β-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-β- 1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multifunctional enzyme possessing endo-β-1,4-xylanase activity together with β-1,3/β-1,4- glucanase activity, which exhibited its highest xylanolytic activity at pH 9.0 and 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylosebased polysaccharides to the XylH were assessed to be as follows: oat spelts xylan > beechwood xylan > birchwood xylan > wheat arabinoxylan. rXylH was also able to readily cleave p-nitrophenyl (pNP) cellobioside and pNP-xylopyranoside, but did not hydrolyze other pNP-sugar derivatives, xylobiose, or hexose-based materials. Enzymatic hydrolysis of birchwood xylan resulted in the product composition of xylobiose (71.2%) and xylotriose (28.8%) as end products.
참고문헌 (39)
- Adlakha N, "Synthesis and characterization of chimeric proteins based on cellulase and xylanase from an insect gut bacterium", Appl. Environ. Microbiol, 77, pp.4859~4866 (2011)
- Ali MK, "Characterization of thermostable Xyn10A enzyme from mesophilic Clostridium acetobutylicum ATCC 824", J. Ind. Microbiol. Biotechnol, 32, pp.12~18 (2005)
- Brune A, "Microecology of the termite gut: structure and function on a microscale", Curr. Opin. Microbiol, 3, pp.263~269 (2000)
- Calderón-Cortés N, "Endogenous plant cell wall digestion: a key mechanism in insect evolution", Annu. Rev. Evol. Syst, 43, pp.45~71 (2012)
- Cardona CA, "Production of bioethanol from sugarcane bagasse: status and perspectives", Bioresour. Technol, 101, pp.4754~4766 (2010)
- Cazemier AE, "Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae", Appl. Environ. Microbiol, 65, pp.4099~4107 (1999)
- Chen S, "Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis", Bioresour. Technol, 128, pp.145~155 (2013)
- Cheng H-L, "The identification, purification, and characterization of STXF10expressed in Streptomyces thermonitrificans NTU-88", Appl. Microbiol. Biotechnol, 82, pp.681~689 (2009)
- Collins T, "Xylanases, xylanase families and extremophilic xylanases", FEMS Microbiol. Rev, 29, pp.3~23 (2005)
- Dheeran P, "A novel thermostable xylanase of Paenibacillus macerans IIPSP3 isolated from the termite gut", J. Ind. Microbiol. Biotechnol, 39, pp.851~860 (2012)
- Flint HJ, "Polysaccharide utilization by gut bacteria: potential for new insights from genomic analysis", Nature Rev. Microbiol, 6, pp.121~131 (2008)
- Fontes CMGA, "A novel Cellvibrio mixtus family 10 xylanase that is both intracellular and expressed under non-inducing conditions", Microbiology, 146, pp.1959~1967 (2000)
- Gallardo O, "Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: a new subclass of family 10 xylanases", Appl. Microbiol. Biotechnol, 61, pp.226~233 (2003)
- Gírio FM, "Hemicelluloses for fuel ethanol: a review", Bioresour. Technol, 101, pp.4775~4800 (2010)
- Gupta N, "A thermostable extracellular xylanase from alkalophilic Bacillus s p. NG-27", Biotechnol. Lett, 14, pp.1045~1046 (1992)
- HEO, SUNYEON, "Characterization of an Extracellular Xylanase in Paenibacillus sp. HY-8Isolated from an Herbivorous Longicorn Beetle", Journal of Microbiology and Biotechnology, 16(11), pp.1753~1759 (2006), 한국미생물·생명공학회
- Huang S, "Isolation and identification of cellulolytic bacteria from the gut of Holotrichia parallela larvae (Coleoptera: Scarabaeidae)", Int. J. Mol. Sci, 13, pp.2563~2577 (2012)
- Keskar SS, "Chemical modification of a xylanase from a thermotolerant Streptomyces:evidence for essential tryptophan and cysteine residues at the active site", Biochem. J, 261, pp.49~55 (1989)
- Kim DY, "Novel GH10 xylanase, with a fibronectin type 3domain, from Cellulosimicrobium sp. strain HY-13, a bacterium in the gut of Eisenia fetida", Appl. Environ. Microbiol, 75, pp.7275~7279 (2009)
- Kim DY, "Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues", Bioresour. Technol, 101, pp.8814~8821 (2010)
- Kim DY, "Catalytic properties of a GH10 endo-β-1,4-xylanase from Streptomyces thermocarboxydus HY-15 isolated from the gut of Eisenia fetida", J. Mol. Catal. B Enzym, 62, pp.32~39 (2010)
- Kim DY, "Novel modular endo-β-1,4-xylanase with transglycosylation activity from Cellulosimicrobium s p. s train HY-13 that i s homologous to inverting GH family 6 enzymes", Bioresour. Technol, 107, pp.25~32 (2012)
- Li N, "Cloning, expression, and characterization of a new xylanase with broad temperature adaptability from Streptomyces s p. S9", Appl. Microbiol. Biotechnol, 80, pp.231~240 (2008)
- Lombard V, "The carbohydrate-active enzymes database (CAZy)in 2013", Nucleic Acids Res (2014)[DOI]
- Lynd LR, "Microbial cellulose utilization: fundamentals and biotechnology", Microbiol. Mol. Biol. Rev, 66, pp.506~577 (2002)
- Mamo G, "A thermostable alkaline active endo-β-1,4-xylanase from Bacillus halodurans S7: purification and characterization", Enzyme Microb. Technol, 39, pp.1492~1498 (2006)
- MacLeod AM, "The acid", base catalyst in the exoglucanase, Biochemistry, pp.1994, 33[DOI]
- Morrison M, "Plant biomass degradation by gut microbiomes: more of the same or something new?", Curr. Opin. Biotechnol, 20, pp.358~363 (2009)
- Oh H-W, "Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12", Antonie van Leeuwenhoek, 93, pp.437~442 (2008)
- Polizeli MLTM, "Xylanases from fungi: properties and industrial applications", Appl. Microbiol. Biotechnol, 67, pp.577~591 (2005)
- Roberge M, "Characterization of active-site aromatic residues in xylanase A from Streptomyces lividans", Protein Eng, 12, pp.251~257 (1999)
- Shi H, "A novel highly thermostable xylanase stimulated by Ca2+ from Thermotoga thermarum: cloning, expression and characterization", Biotechnol. Biofuels, 6, pp.26~ (2013)
- Shi P, "Paenibacillus sp. strain E18 bifunctional xylanase-glucanase with a single catalytic domain", Appl. Environ. Microbiol, 76, pp.3620~3624 (2010)
- Singh RK, "Molecular cloning and characterization of a GH11 endoxylanase from Chaetomium globosum, and its use in enzymatic pretreatment of biomass", Appl. Microbiol. Biotechnol, 97, pp.7205~7214 (2013)
- Usui K, "A cytoplasmic xylanase (XynX) of Aeromonas caviae ME-1 is released from the cytoplasm to the periplasm by osmotic downshock", J. Biosci. Bioeng, 95, pp.488~495 (2003)
- Wackett LP., "Biomass to fuels via microbial transformations", Curr. Opin. Chem. Biol, 12, pp.187~193 (2008)
- Yan Q, "Properties of a xylanase from Streptomyces matensis being suitable for xylooligosaccharides production", J. Mol. Catal. B Enzym, 58, pp.72~77 (2009)
- Zhou J, "Molecular and biochemical characterization of a novel xylanase from the symbiotic Sphingobacterium sp. TN19", Appl. Microbiol. Biotechnol, 85, pp.323~333 (2009)
- Zolotnitsky G, "Mapping glycoside hydrolase substrate subsites by isothermal titration calorimetry", Proc. Natl. Acad. Sci. USA, 101, pp.11275~11280 (2004)