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Journal of the Korean Chemical Society (JKCS)

ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 45, Number 1
JKCSEZ 45(1)
February 20, 2001 

Cross-Linked Enzyme Crystal(CLEC); Stability of Horse Liver Alcohol Dehydrogenase CLEC against Electron Transfer Mediators

격자화 효소결정; 전자이동 중개체에 대한 알코올 탈수소 격자화 효소결정의 안정도
Kang-Min Lee

효소결정을 격자화하여 안정화한 CLEC은 생촉매제로써 뿐아니라 효소센서로 이용할 수 있다. 전자이동 중개체로 사용되고 있는 PMS는 HLADH에 대하여 가장 효율적인 전자이동 활성도를 가졌다. NQS는 PMS에 비하여 52%, phenothiazine은 37%, ferrocene aldehyde는 35%의 전자 이동 활성도를 가졌다. HLADH는 용액상태에서 PMS, NQS에 대하여 매우 불안정하였다. 반면에 HLADH-CLEC은 용액상태에서 불안정했던 PMS, NQS, ferrocene aldehyde에 대하여 매우 안정하였다.

Stabilized Cross-linking Enzyme Crystals(CLEC) can be used as not only biocatalysts but also as enzyme sensors. PMS(Phenylmethyl Sulfate)was shown more efficience than any other electron mediator transfers toward HLADH(Horse Liver Alcohol Dehydrogenase)that were examined. NQS(naphtoquinonesulphonate), phenothiazine and ferrocene aldehyde had respectively just 52%, 37%, 35% electron transfer efficiency as compared to PMS . HLADH-CLEC was very stable toward elctron transfer mediators such as PMS, NQS and ferrocene aldehyde in which HLADH-solution was unstable.

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