Botrytis cinerea, Sclerotinia libertiana and
Gloeosporium kaki were cultivated in the media containing sugars, peptone, NaNO
3, KH
2PO
4, MgSO
4•7 H
2O and trace of FeCl
3 the initial pH value of which was adjusted at pH 5.4, and the shake culture was continued at 28°C for 3 or 4 days. Arabanase was effectively produced in the cultural solution containing araban or arabinose. The optimum pH value for arabanase action was 3.0 (
B. cinerea, S. libertiana) and 4.0_??_6.0 (
G. kaki). When arabanase of these organisms was acted on beet-araban at 40°C for 24 hrs., L-arabinose was found to be the main product, and the small amount of galactose and oligosaccharide of arabinose were also detected by the method of paper chromatography.
Arabanase was extracted from an enzyme preparation of
Coniothyrium diplodiella and purified by the procedure of rivanol precipitation and column chromatography using DEAE-cellulose. When the purified enzyme of
C. diplodiella was acted on araban, the optimum pH value was 3.6_??_3.8, the main product of enzymatic action was L-arabinose and small amount of galactose was shown in paper chromatogram, but no spot of oligosaccharide could be detected in the same chromatogram. The ratio of hydrolysis of araban reached to 93.5% after the arabanase action was continued at pH 3.6, 30°C, for 96 hrs. Any inhibitory effect could not be shown by the addition of aluminium and iron. This inhibitory result was the same as in case of
Asp. niger mentioned in part V.
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