Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1998-11-16
2000-10-31
Achutamurthy, Ponnathapu
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
435183, 435200, C12N 900, C12N 924, C12N 942
Patent
active
061400971
DESCRIPTION:
BRIEF SUMMARY
TECHNICAL FIELD
The present invention relates to xylanases, particularly to novel mesophilic xylanases derived from a mold Acremonium cellulolyticus.
BACKGROUND ART
Xylan is one of the polysaccharides widely existing in nature, and is classified as hemicellulose among polysaccharides, which are the main constituents of cell walls and peripheral tissues of higher plants, such as cellulose, lignin, hemicelluloses, and pectins. The structure is high-molecular-weight polysaccharide having a main chain polymerized by a .beta.-1,4-xyloside bond with xylose being a unit. In nature, xylan exists not only as homoxylan whose constituent sugar is only xylose but also as heteroxylan such as arabinoxylan in which arabinose branches and is bound to the main chain.
Xylanase is the general name for enzymes catalyzing the hydrolysis of xylan via xylosaccharides and xylobiose finally into xylose, and is roughly categorized into endoxylanase, exoxylanase, and .beta.-xylosidase depending on the action modes. Detailed comparison of these action modes establishes a large kind of enzymes. Therefore, it has been thought that xylan in plant tissues is degraded by a synergistic action of xylanases having a variety of action modes.
Xylanase is utilized for production of xylooligosaccharides or xylose from xylan or a treatment of a biomass. In addition, recently, application of xylanase is progressing in the field of enzymes for feeds and food processing, and various kinds of xylanase are under research and development.
A mold Acremonium cellulolyticus has a property that it produces a cellulase having strong saccharification, and usefulness for feed and silage is reported (See e.g. Japanese Patent Laid-open Pub. Nos. Hei 4-117244 and Hei 7-236431). Cellulase component contained therein is also reported (See e.g. Agric. Biol. Chem. 52, 2493-2501 (1988); ibid. 53, 3359-3360 (1989); ibid. 54, 309-317 (1990)). In addition, the crude enzyme produced by said mold produces xylanase together with cellulase, and some components of the xylanase were reported (See e.g. Agric. Biol. Chem. 51, 65-74 (1987); ibid. 51, 3207-3213 (1987); Report of National Institute of Bioscience and Human-Technology, 1, 37-44 (1993), Japanese Patent Pub. No. Hei 1-21957; and Japanese Patent Laid-open Pub. Nos. Hei 1-171484 and Hei 1-171485).
These reports relate to thermostable xylanase and xylooligosyl transferase, and mesophilic xylanase was not known in detail.
It is preferable to use mesophilic xylanase having an activity from neutral to acidic region and in the mesophilic region, the optimal temperature being up to about 60.degree. C. when it is applied for food or feed. Such mesophilic xylanase, however, has not been known so far.
DISCLOSURE OF THE INVENTION
The inventors conducted exhaustive fractionation/purification of various enzymes constituting the xylanase system derived from Acremonium cellulolyticus so that they found novel active components having optimal activities at the mesophilic region in the enzymes. Based on this finding, the present invention was completed. The object of the present invention is to provide novel mesophilic xylanases effective for food processing, feed, silage, and other purposes.
The present invention provides mesophilic Xylanase I, derived from a mold Acremonium cellulolyticus, having the following properties: xylobiose, xylotriose and so on, 3.5-9.5 (25.degree. C., 2 hours) as determined by saccharifying activity using soluble xylan as a substrate, saccharifying activity using soluble xylan as the substrate, min), electrophoresis, 69,500 as determined by gel filtration chromatography, activity for soluble xylan, 76.6 U/mg-protein as determined by saccharifying activity for insoluble xylan.
The present invention also provides mesophilic Xylanase II, derived from the mold Acremonium cellulolyticus, having following properties: xylobiose, xylotriose and so on, 3.0-9.5 (25.degree. C., 2 hours) as determined by saccharifying activity using soluble xylan as a substrate, saccharifying activity using soluble xylan as a sub
REFERENCES:
patent: 4742005 (1988-05-01), Yamanobe et al.
patent: 4956291 (1990-09-01), Yamanobe et al.
Yamanobe et al., "Purification and Some Properties of a Microcrystalline Cellulose-hydrolyzing Enzyme (Avicelase II) from Fugal Strain Y-94", Agric. Biol. Chem., 52(10), 2493-2501 (1988).
Yamanobe et al., "Purification and Properties of a .beta.-Glucosidase from Fungal Strain Y-94", Agric. Biol. Chem., 53(12), 3359-3360 (1989).
Yamanobe et al., "Some Enzymatic Properties of Endo-1 4-.beta.-glucanase Components from Fungal Strain Y-94", Agric. Biol. Chem., 54(2), 309-317 (1990).
Yamanobe et al., "Isolation of a Cellulolytic Enzyme Producing Microorganism, Culture Conditions and Some Properties of the Enzymes", Agric. Biol. Chem., 51(1), 65-74 (1987).
Mitsuishi et al., "Purification and Properties of Thermostable Xylanases from Mesophilic Fungus Strain Y-94", Agric. Biol. Chem., 51(12), 3207-3213 (1987).
Mitsuishi et al., "Two thermostable .beta.-xylosidases from the mesophilic fungal strain Y-94", Report of National Institute of Bioscience and Human-Technology, 1(1), 37-44 (1993).
Hayashi et al, "Purification and Properties of a Low-Temperature-Active Enzyme Degrading Both Cellulose and Xylan from Acremonium Alcalophilum JCM 7366", Seibutsukogakukaishi, A. alcalophilum JCM 7366, vol. 75, No. 1, pp. 9-14, 1997.
Hayashi et al, Low-Temperature-Active Cellulase Produced by Acremonium Alcalophilum JCM 7366, Seibutsukogakukaishi, A. alcalophilum, vol. 74, No. 1, pp. 7-10 (1996).
Gotoh Shoji
Kono Toshiaki
Mizuno Masako
Nihira Takanori
Okada Gentaro
Achutamurthy Ponnathapu
Japan as represented by Director General of Agency of Industrial
Meiji Seika Kaisha Ltd.
Rao Manjunath
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