Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400 |
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| Authors: | Richard M Broadus J D Haddock |
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| Institution: | (1) Department of Pharmacology and Pathobiology, Royal Veterinary and Agricultural University, DK-1870 Frederiksberg C (Copenhagen), Denmark, DK;(2) Dipartimento di Agrobiologia e Agrochimica, University of Tuscia, Via S. C. De Lellis, I-01100 Viterbo, Italy Tel. +39-761-357269; Fax +39-761-357242 e-mail: federici@unitus.it, IT;(3) Dipartimento di Biologia, Difesa e Biotecnologie Agro-Forestali, University of Basilicata, I-85100 Potenza, Italy, IT |
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| Abstract: | Mucor circinelloides LU M40 and Penicillium aurantiogriseum P 35 produce extracellular β-glycosidases that are active on the cyanogenic glycoside amygdalin. From the culture broths
of M. circinelloides, only one β-glycosidase could be identified, while two different enzymes – both having amygdalase activity – were found in
culture broths of P. aurantiogriseum. The study of the mechanism of hydrolysis of the β-bis-glycoside amygdalin with purified enzymes from the two organisms indicated
a possible sequential (two-step) reaction. In all cases, the first step of hydrolysis from amygdalin to prunasin was very
rapid, while the second step from prunasin to cyanohydrin was much slower. No cyanohydrin lyase activity was found in the
culture broths of either fungus.
Received: 16 May 1997 / Accepted: 11 September 1997 |
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| Keywords: | Penicillium aurantiogriseum Mucor circinelloides Fungal amygdalases Hydrolysis mechanism |
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