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Thermostability of β‐xylosidase from Aspergillus sydowii MG49
Author(s) -
Ghosh Mousumi,
Nanda Geeta
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80887-z
Subject(s) - thermostability , chemistry , food science , biochemistry , enzyme
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 Mg 2+ , Mn 2+ , Co 2+ , Ca 2+ and Zn 2+ while, on the other hand Cu 2+ 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.