ISSN:
1432-072X
Keywords:
Key wordsα-l-Rhamnosidase
;
l-rhamnose
;
Pseudomonas paucimobilis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract α-l-Rhamnosidase was extracted and purified from the cells of Pseudomonas paucimobilis FP2001 with a 19.5% yield. The purified enzyme, which was homogeneous as shown by SDS-PAGE and isoelectric focusing, had a molecular weight of 112,000 and an isoelectric point of 7.1. The enzyme activity was accelerated by Ca2+ and remained stable for several months when stored at –20 °C. The optimum pH was 7.8; the optimum temperature was 45 °C. The K m, V max and k cat for p-nitrophenyl α-l-rhamnopyranoside were 1.18 mM, 92.4 μM · min–1 and 117,000 · min–1, respectively. Examination of the substrate specificity using various synthetic and natural l-rhamnosyl glycosides showed that this enzyme had a relatively broader substrate specificity than those reported so far.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050009
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