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L-Arabinose is a major composition of some plant materials; therefore the metabolic pathway of L-arabinose has been identified mainly in microbes which degrade plant materials. Currently, three different pathways for L-arabinose degradation are known. Many bacteria including Escherichia coli convert L-arabinose to D-xylulose phosphate, which is entered into the pentose
phosphate pathway. Some fungi convert L-arabinose to L-arabinitol by using aldose reductase and then D-xylulose phosphate is produced. In addition, a recent study showed that Azospirillum brasiliense converts L-arabinose to α-ketoglutarate via non-phosphorylated pathway composed of five enzymatic steps. The first step of this pathway is catalyzed by L-arabinose dehydrogenase (Abra_AraDH).1) Recently, we found a novel L-arabinose dehydrogenase
(Bcep_AraDH) from Burkholderia cepacia KCTC 2966. To characterize this enzyme, the gene encoding B. cepacia L-arabinose dehydrogenase was cloned and expressed in E.coli BL21(DE3). The enzyme was purified using Ni-NTA column and its kinetic parameters were determined using various sugars as substrates. There was no sequence homology between Abra_AraDH and Bcep_AraDH. It was also found that Bcep_AraDH could utilize five different
sugars; L-arabinose, D-galactose, D-fucose, D-glucose and D-xylose. We postulated that the enzyme specificity is related to the structural property of sugars

저자

• In Chol Kim [ Department of Chemical Engineering, Pohang University Science and Technology ]
• Sun Bok Lee [ Department of Chemical Engineering, Pohang University Science and Technology ]

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576