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자료유형
학술저널
저자정보
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한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제17권 제8호
발행연도
2007.1
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1,291 - 1,299 (9page)

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Two β-1,4-glucanases (DI and DIII fractions)were purified to homogeneity from the culture filtrate of acellulolytic bacteria, Cellulomonas sp. CS1-1, which wasclassified as a novel species belonging to Celulomonas udabased on chemotaxanomic and phylogenetic analyses. Themolecular mass was estimated as 50,000 Da and 52,000 Dafor DI and DIII, respectively. Moreover, DIII was identifiedas a glycoprotein with a pI of 3.8, and DI was identified as anon-glycoprotein with a pI of 5.3. When comparing the ratioof the CMC-saccharifying activity and CMC-liquefying activity,whereas DIII exhibited a low slope, characteristic of anexoglucanase. The substrate specificity of the purified enzymesrevealed that DI efficiently hydrolyzed CMC as wel as xylan,whereas DIII exhibited a high activity on microcrystalinecelluloses, such as Sigmacells. A comparison of the hydrolysispaterns for pNP-glucosides (DP 2-5) using an HPLC analysisdemonstrated that the halosidic bond 3 from the nonreducingend was the preferential cleavage site for DI, whereas bond 2,from which the cellobiose unit is split off, was the preferentialsequences for the purified enzymes were 1Ala-Gly-Ser-Thr-Leu-Gln-Ala-Ala-Ala-Ser-Glu-Ser-Gly-Arg-Tyr15- for DI and1Ala-Asp-Ser-Asp-Phe-Asn-Leu-Tyr-Val-Ala-Glu-Asn-Ala-Met-Lys15- for DIII. The apparent sequences exhibited highsequence similarities with other bacterial β-1,4-glucanases aswel as β-1,4-xylanases.

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