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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.


Related in: MedlinePlus

Stabilities of the Purified Enzymes toward 10-DAXP.(a) Thermal stability of the 10-DAXP xylosidase activity of the two purified enzymes. (b) stability of the 10-DAXP xylosidase activity of the two purified enzymes under reaction conditions.
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f4: Stabilities of the Purified Enzymes toward 10-DAXP.(a) Thermal stability of the 10-DAXP xylosidase activity of the two purified enzymes. (b) stability of the 10-DAXP xylosidase activity of the two purified enzymes under reaction conditions.

Mentions: To determine the overall catalytic capacity of the purified enzymes, their stabilities were also investigated. At 30 °C and 10% methanol, the half-life of Xyl_I was approximately 214 hours, in sharp contrast with only 6 hours for the isolated subunit Xyl_S (Fig. 4).


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)

Stabilities of the Purified Enzymes toward 10-DAXP.(a) Thermal stability of the 10-DAXP xylosidase activity of the two purified enzymes. (b) stability of the 10-DAXP xylosidase activity of the two purified enzymes under reaction conditions.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f4: Stabilities of the Purified Enzymes toward 10-DAXP.(a) Thermal stability of the 10-DAXP xylosidase activity of the two purified enzymes. (b) stability of the 10-DAXP xylosidase activity of the two purified enzymes under reaction conditions.
Mentions: To determine the overall catalytic capacity of the purified enzymes, their stabilities were also investigated. At 30 °C and 10% methanol, the half-life of Xyl_I was approximately 214 hours, in sharp contrast with only 6 hours for the isolated subunit Xyl_S (Fig. 4).

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