Thermostability of β‐xylosidase from Aspergillus sydowii MG49

FEBS Letters

Nanda, Geeta¹  Ghosh, Mousumi¹ 

[1] Department of Microbiology, Bose Institute, P-1112, C.I.T. Scheme, VII - M, Calcutta - 700054, India

关键词: β-Xylosidase;    Thermostabilization;    Aspergillus sydowii;   

DOI  :  10.1016/0014-5793(93)80887-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Heating of Aspergillus β-xylosidase at 85°C ± 1°C and pH 5.5–6.0 (optimum for activity), causes irreversible, covalent thermoinactivation of the enzyme, involving oxidation of the thiol groups that are required for catalysis. Exogenous addition of cysteine, DTT, GSH and mercaptoethanol stabilizes the enzyme by extending its half-life. A similar effect is also exhibited by bivalent cations like Mg²⁺, Mn²⁺, Co²⁺, Ca²⁺and Zn²⁺ while, on the other hand Cu²⁺ accelerates thermoinactivation. Chemical modification of crude β-xylosidase with cross-linking agents like glutaraldehyde or covalent immobilization to a nonspecific protein like gelatin and BSA also enhances enzyme thermostability. These results suggest that addition of thiols and bivalent metal ions to a crude β-xylosidase preparation or immobilization/chemical modification enhances its thermal stability, thus preventing loss of catalytic activity at elevated temperatures.

【 授权许可】

Unknown