Rhodococcus pyridinovorans MW3 was isolated from an arable land of manioc from the Congo for its ability to transform acrylonitrile to acrylamide. This strain contains a cobalt nitrile hydratase (NHase) showing high sequence homology with NHases so far described. The specific NHase activity was 97 U mg(-1) dry wt. NHase production by R. pyridinovorans MW3 was urea and Co-dependent. The NHase was active for acrylamide up to 60% (w/v) indicating its potential for acrylamide production.

The endocellular enzyme beta-glucosidase of Candida cacaoi was purified by ion-exchange chromatography and gel filtration. The molecular weight was 220 +/- 10 kDa; its optimum pH was between 4 and 5.5 and its optimum temperature was 60 degrees C. This enzyme was active against soluble glucosides tested with beta(1-2), beta(1-3), beta(1-4) and even alpha(1-4) and alpha(1-6) and was inhibited by D-glucono-delta-lactone. The enzyme was constitutive but its synthesis was repressed by glucose.

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