Purifications and Properties of Galactanases from Alkalophilic Bacillus sp. S-2 and S-39(Microbiology & Fermentation Industry)

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Two galactanases (galactanase S-2 and S-39) were purified to homogeneous states from culture filtrates of alkalophilic Bacillus sp. S-2 and S-39, respectively. The galactanase from Bacillus sp. S-2 were purified by ammonium sulfate precipitation, chromatography on DEAE-Cellulofine, and by gel filtration on Cellulofine GC-200m. The enzyme had a molecular weight (SDS-PAGE) of 40,000 and isoelectric point of 8.6. It was most active at pH 10 and 50℃, and was stable between pH 7 and 12 (at 20℃ for 15 hr), and below 45℃ (at pH 10 for 15 min). The galactanase from Bacillus sp. S-39 was purified by ammonium sulfate precipitation and chromatographies on DEAE-Toyopearl 650M and CM-Toyopearl 650M. The enzyme had a molecular weight (SDS-PAGE) of 36,000 and isoelectric point of 7.1. It was most active at pH 4 and 40℃, and was stable between pH 5 and 12 (at 20℃ for 15 hr), and below 60℃ (at pH 4 for 15 min). Both enzymes hydrolyzed soybean galactan to produce galactooligosaccharides with very little galactose, but did not attack larch wood arabinogalactan. These enzymes were both referred to as endo-β-1,4-galactanases (EC 3.2.1.89).
社団法人日本農芸化学会の論文
1991-05-23