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Thermal stabilization by polyols of β-xylanase from Bacillus amyloliquefaciens

✍ Scribed by Javier D. Breccia; Ana C. Morán; Guillermo R. Castro; Faustino Siñeriz

Book ID
101263183
Publisher
Wiley (John Wiley & Sons)
Year
1998
Tongue
English
Weight
227 KB
Volume
71
Category
Article
ISSN
0268-2575

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✦ Synopsis

PuriÐed endo-b-1,4-xylanase of Bacillus amyloliquefaciens MIR 32 retained 100% of its activity after 4 days of incubation at 50¡C. Sorbitol (400 mg cm~3) produced a 63-fold increase in the half-life of the enzyme at 65¡C, which was only 29 min at this temperature in the absence of the polyol. This thermal stabilizing activity increased exponentially in respect to sorbitol concentration in the range 250È400 mg cm~3 and was dependent on the pH, showing a maximum at pH values between 5É25 and 8É0. The circular dichroism (CD) thermal scanning proÐle (50¡C h~1) at 224 nm showed that changes in the secondary structure of xylanase started at 65¡C, while in the presence of sorbitol (400 mg cm~3) these modiÐcations started at 80¡C. This study indicated that sorbitol might be a valuable stabilizer for the use of b-xylanase from B. amyloliquefaciens at high temperatures.

1998 SCI (

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