Purification and Some Properties of Endo-l,4-<i>β</i>-<scp>d</scp>-xylanase from a Fresh-water Mollusc,<i>Pomacea insularus</i>(de Ordigny)

Yamaura, Izumi; Koga, Takaki; Matsumoto, Toshihiko; Kato, Tsuyoshi

doi:10.1271/bbb.61.615

Cited by 32 publications

(16 citation statements)

References 8 publications

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“…Some members of higher animals, including fresh water mollusc, are able to produce xylanases. 43 There are lots of reports on microbial xylanases starting from 1960: Nevertheless, these reports have given prime importance to plant pathology-related studies. 25,44 Only during 1980s has the great impact of xylanases been tested in the area of biobleaching.…”

Section: Xylanolytic Enzymesmentioning

confidence: 99%

“…that grow at a temperature higher than 80°C could be easily purified by the inclusion of one additional step of heating. 80 Use of cellulose materials as the matrix in column chromatography is impaired by the fact that certain xylanases 43 have cellulose binding domains, which will interact with the normal elution process. 77 Takahashi et al 97 purified a low molecularweight xylanase (23 kDa) from Bacillus sp.…”

Section: Purification and Properties Of Xylanasesmentioning

confidence: 99%

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Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application

Subramaniyan

Prema

2002

Critical Reviews in Biotechnology

552

275

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Xylanases are hydrolases depolymerizing the plant cell wall component xylan, the second most abundant polysaccharide. The molecular structure and hydrolytic pattern of xylanases have been reported extensively and the mechanism of hydrolysis has also been proposed. There are several models for the gene regulation of which this article could add to the wealth of knowledge. Future work on the application of these enzymes in the paper and pulp, food industry, in environmental science, that is, bio-fueling, effluent treatment, and agro-waste treatment, etc. require a complete understanding of the functional and genetic significance of the xylanases. However, the thrust area has been identified as the paper and pulp industry. The major problem in the field of paper bleaching is the removal of lignin and its derivatives, which are linked to cellulose and xylan. Xylanases are more suitable in the paper and pulp industry than lignin-degrading systems.

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Section: Xylanolytic Enzymesmentioning

confidence: 99%

Section: Purification and Properties Of Xylanasesmentioning

confidence: 99%

Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application

Subramaniyan

Prema

2002

Critical Reviews in Biotechnology

552

275

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“…This battery is usually composed of b-1,4-endoxylanase, b-D-xylosidase, a-L-arabinofuranosidase, a-D-glucuronidase, acetylxylan esterase, and phenolic acid esterase (Sunna and Antranikian, 1997). These enzymes act cooperatively to convert xylan into its constituting sugars (Rahman et al, 2003;Tuncer and Ball, 2003), and they have been reported to occur widely in microorganisms (Kulkarni et al, 1999;Subramaniyan and Prema, 2000;Beg et al, 2001), fungi (Coughlan and Hazlewood, 1993;Sunna and Antranikian, 1997), and animals (Yamaura et al, 1997). Side chain cleaving enzymes, such as a-L-arabinofuranosidase, a-D-glucuronidase, and acetylxylan esterase, remove substituent functional groups of heteroxylans.…”

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confidence: 99%

Purification and Characterization of Enzymes Exhibiting β-d-Xylosidase Activities in Stem Tissues of Arabidopsis

et al. 2004

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This work describes the purification and characterization of enzymes that exhibit b-D-xylosidase activity in stem tissues of Arabidopsis. This is the first detailed investigation that concerns the characterization of catalytic properties and sequence identity of enzymes with b-D-xylosidase activities in a dicotyledonous plant. Three different enzymes, ARAf, XYL4, and XYL1 with apparent molecular masses of 75, 67, and 64 kD, respectively, were purified to homogeneity. ARAf was identified as a putative a-L-arabinofuranosidase, and XYL4 and XYL1 as putative b-D-xylosidases using matrix-assisted laser-desorption ionization time of flight. ARAf belongs to family 51 and XYL4 and XYL1 to family 3 of glycoside hydrolases. ARAf and XYL1 have highest specificity for p-nitrophenyl-a-L-arabinofuranoside and XYL4 for p-nitrophenyl-b-D-xylopyranoside and natural substrates such as xylobiose and xylotetraose. XYL4 was shown to release mainly D-Xyl from oat spelt xylan, rye arabinoxylan, wheat arabinoxylan, and oligoarabinoxylans. ARAf and XYL1 can also release D-Xyl from these substrates but less efficiently than XYL4. Moreover, they can also release L-Ara from arabinoxylans and arabinan. Overall, the results indicate that XYL4 possesses enzymatic specificity characteristic for a b-D-xylosidase, while ARAf and XYL1 act as bifunctional a-L-arabinofuranosidase/b-D-xylosidases. Analysis of the activity of these three enzymes in stem tissues at different stages of development has shown that young stems possess the highest activities for all three enzymes in comparison to the activities of the enzymes present in stems at older stages of development. High enzyme activities are most likely related to the necessary modifications of cell wall structure occurring during plant growth. Plant cells are surrounded by an extracellular matrix known as the cell wall. The regulation of cell wall morphology and composition is important for the determination of cell size and shape, cellular interactions with the environment, mechanical resistance, and defense against pathogen attacks (Reiter, 2002). The cell wall is also involved in plant growth and development (Stolle-Smits et al., 1999;Obel et al., 2002). In addition, although cell walls consist mainly of polysaccharides broadly classified as celluloses, hemicelluloses, and pectins, their constitution varies, not only from plant to plant, but also in different tissues of the same plant (Heredia et al., 1995;Cosgrove, 1997;Popper and Fry, 2003). A coordinated series of biochemical processes occur during plant development resulting in the biosynthesis and degradation of cell wall components. Consequently, numerous enzymes must be implicated in these processes (Heredia et al., 1995;Cosgrove, 1997;Stolle-Smits et al., 1999;Obel et al., 2002;Reiter, 2002;Popper and Fry, 2003). However, to date, little information is available concerning such enzymes, their mode of action, and their physiological role. Increased research interest has focused on enzymes involved in the metabolism of hemicelluloses in ...

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“…In previous reports, Cu 2? is considered as a strong inhibitor in the industrial application of xylanase (Yamaura et al 1997). However, Bpu XynA retained approximately 81% activity in the presence of 1 mM Cu 2?…”

Section: Discussionmentioning

confidence: 99%

Cloning, expression and characterization of glycoside hydrolase family 11 endoxylanase from Bacillus pumilus ARA

Shao

2011

Biotechnol Lett

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An endoxylanase gene, xynA, was cloned from Bacillus pumilus ARA and expressed in Escherichia coli. The open reading frame of the xynA gene was 687 bp encoding a signal peptide and a mature xylanase with a molecular mass of 23 kDa. The enzyme was categorized as a glycosyl hydrolase family 11 member based on the sequence analysis of the putative catalytic domain. The recombinant XynA (Bpu XynA) was purified to homogeneity by Ni-NTA and ion exchange chromatography on DEAE-Sepharose FF. The enzyme exhibited highest activity at pH 6.6 and 50°C. The purified Bpu XynA was stable for at least 2 h at 45°C, and retained over 50% residual activity after being incubated at 60°C for 1 h. The activity of the xylanase was not significantly affected by metal ions and EDTA. The K ( m ) and K ( cat ) /K ( m ) of Bpu XynA for oat-spelt xylan were 5.53 mg/ml and 10.14 ml/mg s at 50°C and pH 6.6. The main product of hydrolysis by Bpu XynA was xylooligosaccharide. The results revealed that the consumption of grass xylan by B. pumilus ARA depended on the synergistic reactions of Bpu XynA and Bpu arabinosidase, and that a typical GH11 xylanase e.g. Tla XynA had capability to remove the side chain of xylan. The properties Bpu XynA make it promising for application in the production of Bifidobacterium growth-promoting factors and in feed industry.

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Purification and Some Properties of Endo-l,4-β-d-xylanase from a Fresh-water Mollusc,Pomacea insularus(de Ordigny)

Cited by 32 publications

References 8 publications

Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application

Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application

Purification and Characterization of Enzymes Exhibiting β-d-Xylosidase Activities in Stem Tissues of Arabidopsis

Cloning, expression and characterization of glycoside hydrolase family 11 endoxylanase from Bacillus pumilus ARA

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