• 한국미생물·생명공학회지
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• 제23권6호
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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.

• 한국식품영양학회지
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• 제10권4호
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• pp.497-502
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• 1997

대두 및 두유박의 주요 다당류인 대두 arabinogalactan(SAG)을 이용하여 갈락토올리고당을 생산하고자 SAG 가수분해효소인 $\beta$-1, 4-galactanase를 이용하여 대두 갈락토올리고당(SOS)의 생산조건 및 그 특성을 연구 검토하였다. SOS는 SAG 1%(w/v), pH 8.0, 5$0^{\circ}C$인 조거에서 $\beta$-1, 4-galactanase를 20unit/g SAG를 첨가하여 24-40시간 반응하여 생산하였다. 생산된 SOS 용액(75%)은 11,000cp의 점도를 나타내어 같은 농도의 설탕용액 140cp의 값에 비해 80배 큰 값을 나타내었다. 점도의 온도의존성은 5$0^{\circ}C$ 이하에서는 온도의존 함수(B) 값이 11,037 cp.K로 설탕용액의 2,760보다 약 4.6배 크지만 5$0^{\circ}C$ 이상에서는 3,400으로 큰 차이를 보이지 않았다. 또한 올리고당의 농도가 50 Brix 이하에서는 설탕용액의 점도 20-30 cp와 유사한 20-40cp로 차이를 보이지 않지만 농도가 증가함에 따라 차이가 커져 Brix 70에서는 1,280cp로 설탕용액의 90cp보다 15배 높은 값을 나타내었다. 생산된 SOS는 pH 및 온도에 대해 매우 안정하여 pH 3,14$0^{\circ}C$인 조건하에서도 분해로 인하여 생산되는 galactose가 없었다.

• 한국미생물·생명공학회지
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• 제23권6호
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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%.