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Functional and structural properties of a novel cellulosome-like multienzyme complex: efficient glycoside hydrolysis of water-insoluble 7-xylosyl-10-deacetylpaclitaxel.

Dou TY, Luan HW, Ge GB, Dong MM, Zou HF, He YQ, Cui P, Wang JY, Hao DC, Yang SL, Yang L - Sci Rep (2015)

Bottom Line: This cellulosome-like multienzyme complex has a novel structure distinct from the well-documented ones.The key catalytic subunit responsible for the β-xylosidase activity against 10-DAXP is identified to be a novel protein, indicating a new glycoside hydrolase (GH) family.The pioneering work described here offers a novel nanoscale biocatalyst for the production of biofuels and chemicals from renewable plant-based natural resources.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Pharmaceutical Resource Discovery, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.

ABSTRACT
Cellulosome is a kind of multienzyme complex that displays high activity, selectivity, and stability. Here, we report a novel, non-cellulolytic, cellulosome-like multienzyme complex that produced by the Cellulosimicrobium cellulans wild-type strain F16 isolated from soil microflora. This multienzyme complex, with excellent catalytic efficiency of kcat 13.2 s(-1) to remove the C-7 xylosyl group from 7-xylosyl-10-deacetylpaclitaxel (10-DAXP), has an outstanding tolerance against organic solvents and an excellent general stability, with the long half-life of 214 hours. This cellulosome-like multienzyme complex has a novel structure distinct from the well-documented ones. The key catalytic subunit responsible for the β-xylosidase activity against 10-DAXP is identified to be a novel protein, indicating a new glycoside hydrolase (GH) family. The pioneering work described here offers a novel nanoscale biocatalyst for the production of biofuels and chemicals from renewable plant-based natural resources.

No MeSH data available.


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Morphology of the Purified Nanoscale Biocatalyst Xyl_I and Its Substrate Specificity.(a) Transmission electron microscopy analysis of the Multi protein complex that purified from the supernatant of the culture, negatively stained by phosphotungstic acid; (b) Substrate specificity of the purified enzymes.
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f1: Morphology of the Purified Nanoscale Biocatalyst Xyl_I and Its Substrate Specificity.(a) Transmission electron microscopy analysis of the Multi protein complex that purified from the supernatant of the culture, negatively stained by phosphotungstic acid; (b) Substrate specificity of the purified enzymes.

Mentions: The essential subunit, responsible for the 10-DAXP β-xylosidase activity of the multiprotein component Xyl_I, was isolated from the proteinase K partially digested mixture of Xyl_I and purified to homogeneity, with a purification factor of 31.8 (Supplementary Table 1, Fig. 1). This isolated subunit, i.e., Xyl_S, also showed 10-DAXP xylosidase activity. Moreover, Xyl_S also showed “double eyelid” bands on the native polyacrylamide gel with the further-migrated (higher Rf value) band to be the active form toward MUX (Supplementary Fig. 1b), which was very similar to that of Xyl_IV.


Functional and structural properties of a novel cellulosome-like multienzyme complex: efficient glycoside hydrolysis of water-insoluble 7-xylosyl-10-deacetylpaclitaxel.

Dou TY, Luan HW, Ge GB, Dong MM, Zou HF, He YQ, Cui P, Wang JY, Hao DC, Yang SL, Yang L - Sci Rep (2015)

Morphology of the Purified Nanoscale Biocatalyst Xyl_I and Its Substrate Specificity.(a) Transmission electron microscopy analysis of the Multi protein complex that purified from the supernatant of the culture, negatively stained by phosphotungstic acid; (b) Substrate specificity of the purified enzymes.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4562250&req=5

f1: Morphology of the Purified Nanoscale Biocatalyst Xyl_I and Its Substrate Specificity.(a) Transmission electron microscopy analysis of the Multi protein complex that purified from the supernatant of the culture, negatively stained by phosphotungstic acid; (b) Substrate specificity of the purified enzymes.
Mentions: The essential subunit, responsible for the 10-DAXP β-xylosidase activity of the multiprotein component Xyl_I, was isolated from the proteinase K partially digested mixture of Xyl_I and purified to homogeneity, with a purification factor of 31.8 (Supplementary Table 1, Fig. 1). This isolated subunit, i.e., Xyl_S, also showed 10-DAXP xylosidase activity. Moreover, Xyl_S also showed “double eyelid” bands on the native polyacrylamide gel with the further-migrated (higher Rf value) band to be the active form toward MUX (Supplementary Fig. 1b), which was very similar to that of Xyl_IV.

Bottom Line: This cellulosome-like multienzyme complex has a novel structure distinct from the well-documented ones.The key catalytic subunit responsible for the β-xylosidase activity against 10-DAXP is identified to be a novel protein, indicating a new glycoside hydrolase (GH) family.The pioneering work described here offers a novel nanoscale biocatalyst for the production of biofuels and chemicals from renewable plant-based natural resources.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Pharmaceutical Resource Discovery, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.

ABSTRACT
Cellulosome is a kind of multienzyme complex that displays high activity, selectivity, and stability. Here, we report a novel, non-cellulolytic, cellulosome-like multienzyme complex that produced by the Cellulosimicrobium cellulans wild-type strain F16 isolated from soil microflora. This multienzyme complex, with excellent catalytic efficiency of kcat 13.2 s(-1) to remove the C-7 xylosyl group from 7-xylosyl-10-deacetylpaclitaxel (10-DAXP), has an outstanding tolerance against organic solvents and an excellent general stability, with the long half-life of 214 hours. This cellulosome-like multienzyme complex has a novel structure distinct from the well-documented ones. The key catalytic subunit responsible for the β-xylosidase activity against 10-DAXP is identified to be a novel protein, indicating a new glycoside hydrolase (GH) family. The pioneering work described here offers a novel nanoscale biocatalyst for the production of biofuels and chemicals from renewable plant-based natural resources.

No MeSH data available.


Related in: MedlinePlus