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J. Biochem, 1982, Vol. 91, No. 4 1181-1186
© 1982 Japanese Biochemical Society

research-article

Purification and Characterization of a Novel Exo-ß-Mannanase from Aeromonas sp. F-25

Toshiyoshi ARAKI and Manabu KITAMIKADO

Department of Fisheries, Faculty of Agriculture, Kyushu University Hakozaki, Higashi-ku, Fukuoka, Fukuoka 812

A novel exo-ß-mannanase (1,4-ß-D-mannan mannobiohydrolase) was isolated from the culture fluid of strain No. F-25 of Aeromonas hydrophila subspecies anaerogenes, and purified about 4,000-fold by ammonium sulfate precipitation and successive column chromatographies. The final enzyme preparation appeared to be homogeneous on polyacrylamide gel electrophoresis. The enzyme hydrolyzed the ß-1,4-mannan link in polysaccharides of three or more ß-1,4-linked D-mannose units. The enzyme had a molecular weight of 64,000, pI of 5.9, pH optimum of 6.0, and was stable in a pH region of 5.0 to 8.5 and at temperatures below 45°C. The Km values of the enzyme were 5.1 x 10–4 M for mannotriose, 2.4 x 10–4 M for mannotet-raose and 1.3 x 10–4 M for mannopentaose. The enzyme attacked codium and coffee mannans to give only mannobiose. Mannobiosyl- and mannotetraosyl-mannitol were hydrolyzed to produce mannobiose and mannitol, while mannobiose and mannosylmannitol were released from mannotriosylmannitol. The enzyme did not act on mannobiose, p-nitrophenyl-ß-D-mannoside, konjac glucomannan, or guar gum galactomannan. Furthermore, the enzyme catalyzed a transglycosylation reaction.


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