This research was funded by a Stategic Operating Grant from the Natural Sciences and Engineering Research Council of Canada.
Purification and characterization of a CIostfidium perfringens α-galactosidase
Version of Record online: 25 AUG 2006
Journal of Food Science
Volume 50, Issue 2, pages 518–522, March 1985
How to Cite
DURANCE, T. and SKURA, B. (1985), Purification and characterization of a CIostfidium perfringens α-galactosidase. Journal of Food Science, 50: 518–522. doi: 10.1111/j.1365-2621.1985.tb13441.x
- Issue online: 25 AUG 2006
- Version of Record online: 25 AUG 2006
- Ms reveived 6/13/84, revised 10/31/84, accepted 11/8/84
Of 21 strains of C. perfringens tested for hydrolysis of α-galactosides, 10 utilized either raffinose or melibiose while 2 utilized both sugars. Spore production in Duncan Strong medium was superior in the presence of raffinose as opposed to starch in 12 out of 21 strains. C. perfringens M34 yielded 1.2 units of α-galactosidase/g washed cells. This enzyme had an isoelectric point of 5.6 and a pH optimum for hydrolysis of PNPG of 6.3. Native and monomer molecular weights were 96,000 and 46,000 daltons respectively. Km was 0.20 ± 0.02mM PNPG. Heat stability of the enzyme decreased as purity increased. This trend was partially reversed by addition of 2-mercaptoethanol, NADH, cysteine, and/or bovine serum albumin to reaction mixture.