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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제17권 제11호
- 발행연도
- 2007.1
- 수록면
- 1,789 - 1,796 (8page)
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A β-glucosidase with the molecular mass of
160,000 Da was purified to homogeneity from cell extract of a
cellulolytic bacterium, Cellulomonas uda CS1-1. The kinetic
parameters (Km and Vmax) of the enzyme were determined
with pNP-cellooligosccharides (DP 1-5) and cellobiose. The
molecular orbital theoretical studies on the cellulolytic reactivity
between the pNP-cellooligosaccharides as substrate (S)
molecules and the purified β-glucosidase (E) were conducted
by applying the frontier molecular orbital (FMO) interaction
theory. The results of the FMO interaction between E and S
molecules verified that the first stage of the reaction was
induced by exocyclic cleavage, which occurred in an electrophilic
reaction based on a strong charge-controlled reaction between
the highest occupied molecular orbital (HOMO) energy of the
S molecule and the lowest occupied molecular orbital
(LUMO) energy of the hydronium ion (H3O+), more than
endocyclic cleavage, whereas a nucleophilic substitution
reaction was induced by an orbital-controlled reaction between
the LUMO energy of the oxonium ion (SH+) protonated to the
S molecule and the HOMO energy of the H2O2 molecule. A
hypothetic reaction route was proposed with the experimental
results in which the enzymatic acid-catalyst hydrolysis reaction
of E and S molecules would be progressed via SN1 and SN2
reactions. In addition, the quantitative structure-activity
relationships (QSARs) between these kinetic parameters showed
that Km has a significant correlation with hydrophobicity (logP),
and specific activity has with dipole moment, respectively.
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