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a-Galactosidase를 생산하는 Bacillus licheniformisYB-42의 분리와 효소 특성

Characterization of Extracellular a-Galactosidase Produced by Bacillus licheniformis YB-42.

최준호|이경섭|이미성|윤기홍|김현숙|소재호
한국미생물·생명공학회 (The Korean Society For Microbiology And Biotechnology)|2004.06|한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)|제32권 제2호|pp. 128-134

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참고문헌

주제분류생물학

초록

가정에서 제조된 된장으로부터 a-galactosidase의 생산균으로 분리된 YB-42는 형태적 특성, 생화학적 성질 및 16S rRNA의 염기서열에 근거하여 Bacillus licheniformis로 동정되었다. B. licheniformis YB-42의 a-galactosidase 활성은 균체내·외에서 모두 관찰되었다. 배양상등액으로부터 DEAE-Sepharose와 Q-Sepharose 컬럼 크로마토그래피를 통해 부분정제한 a-galactosidase을 사용하여 para-nitrophenyl-a-D-galactopyranoside(pNP-aGal)의 가수분해 반응특성을 조사한 결과 45oC와 pH 6.5에서 최대활성을 보였다. Melibiose, raffinose와 stachyose는 부분 정제효소액에 의해 완전히 가수분해 되었으며, 분해산물로 galactose가 생성된 것으로 보아 a-1,6 결합이 분해된다는 것이 확인되었다. 한편 pNP-aGal과 melibiose의 가수분해 활성은 galactose에 의해 가장 크게 저해되었으며, galactose 보다는 낮지만 pNP-aGal의 가수분해 활성이 mannose와 glucose에 의해서도 저해되는 것으로 나타났다.

Abstract

A bacterium producing the a-galactosidase was isolated from Korean soybean paste. The isolate YB-42 has been identified as Bacillus licheniformis on the basis on its 16S rRNA sequence, morphology and biochemical properties. The a-galactosidase activity was detected in both the culture supernatant and the cell extract of B. licheniformis YB-42. The partially purified extracellular a-galactosidase was obtained from the culture supernatant by DEAE-Sepharose column and Q-Sepharose column chromatography. The enzyme showed the maximum activity for hydrolysis of para-nitrophenyl-a-D-galactopyranoside (pNP-aGal) at pH 6.5 and 45oC. It was able to hydrolyze oligomeric substrates such as melibiose, raffinose and stachyose to liberate galactose residue, indicating that the a-galactosidase of B. licheniformis YB-42 hydrolyzed a-1,6 linkage. The hydrolyzing activity of a-galactosidase for both pNP-aGal and melibiose was dramatically decreased by galactose. Both glucose and mannose inhibited the activity for pNP-aGal less than galactose.

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