• Microbiology and Biotechnology Letters
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• v.23 no.6
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• pp.687-694
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• 1995

Alkalophilic Bacillus sp. HJ-12 producing $\beta $-1, 4-D-arabinogalactanase was isolated from soil in the alkalic condition, pH 10.0. $\beta $-1, 4-D-arabinogalactanase was maximaly produced in the medium consisting of 2% soybean arabinogalactan (SAG), 0.5% yeast extract, 0.5% polypeptone, 0.5% NaCl, 0.1% K$_{2}$HPO$_{4}$, 0.02% MgSO$_{4}$$\cdot $7H$_{2}$O, 0.1% Na$_{2}$CO$_{3}$ under the aerobic condition (pH 8.2). $\beta $-1, 4-D-arabinogalactanase is inducible enzyme so that its activity has been increased 10 fold in the SAG medium than in the glucose medium. Through the ammonium sulfate precipitation, DEAE- Sephadex A-50 ion chromatography, and Sephadex G-75 gel chromatography procedures, this enzyme was purified with a single protein of 11% vield and 110 fold's purity. $\beta $-1, 4-D-arabinogalactanase is endo type enzyme producing ollgosaccharide from SAG.

• The Korean Journal of Food And Nutrition
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• v.10 no.4
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• pp.497-502
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• 1997

For the purpose of enzymatic production of galactooligosaccharides from soybean arabinogalactan (SAG) hydrolysis, the $\beta$-1, 4-D-arabinogalactanase($\beta$-1, 4-galactanase) from Bacillus sp. HJ-12 was used. The soybean galactooligosaccharides(SOS) were optimally produced in SAG 1%(w/v), pH 8.0, 5$0^{\circ}C$, $\beta$-1, 4-galactanase 20unit/g SAG and 24-40 hour reaction conditions. The produced galactooligosaccharides had visocity of 11,000 cp at 75%(w/v), $25^{\circ}C$. The viscosity of galactooligosaccharides was 80 fold increasing value than that of sucrose solution. Temperature dependence of viscosity of SOS was 4.6 fold higher value than surose solution below than 5$0^{\circ}C$. Less than 50 Brix, the viscosity of SOS was similar with sucrose solution(20-40 cp), but increasing of concentration, the difference of viscosity between SOS and sucrose solution was increased. And, SOS was very stable at pH and temperature.

• Microbiology and Biotechnology Letters
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• v.23 no.6
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• pp.710-716
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• 1995

$\beta $-1, 4-D-arabinogalactanase isolated from alkalophilic Bacillus sp. HJ-12, approximate Mw 42 kDa, was generally stable in the range of pH 6-10 and below 50$\circ$C and its highest activity was observed at 60$\circ$C with pH 7-9. The isolated $\beta $-1, 4-D-arabinogalactanase specifically hydrolyzed $\beta $-1, 4-galactosyl linkage that is the major structure of soybean arabinogalactan (SAG) but not $\beta $-1, 3-galactosyl linkage of the other polysaccharides. K. was estimated as 0.67 mg/ml by the method of Hanes-Woolf plot. No metals and chemical reagents inhibited the enzyme activity but urea did. The active site of this enzyme assumed to be tryptophan residue. The hydrolysis products from SAG, assayed by gel chromatography, TLC and HPLC, were predominantly galactotetraose (Gal$_{4}$) and triose (Gal$_{3}$) with a small portion. $\beta $-1, 4-D-arabinogalactanase hydrolyzed ONPG as well as SAG, and the degree of hydrolysis of SAG was 15% which is lower than that by the other $\beta $-1, 4-galactanases from different sources. SAG treated with this enzyme resulted in the reduction of specific viscosity up to 70%.