원문정보
Kinetics on the Specificity of Enzymatic Hydrolysis of Chitin
초록
영어
Hydrolysis and adsorption reversibility experiments were run for initial enzyme activity of 4.48, 9.65, 11.19 and 17.14U/mL at a temperature 30℃. The chitin particle size corresponded to a mean particle diameter of 0.127mm, and the initial concentration of chitin was 10mg/mL. After approximately 2hrs, the enzyme activity remained constant in a speudo-steady state. The amounts in the bulk [E] and the amounts of enzyme adsorbed on the chitin surface [E] are plotted on Lineweaver-Burk plot to yield a linear relationship with a correlation coefficient of 0.99, a slope of 2.79cm and an intercept of 0.08cm2/U. From this parameters, the values of [ET] and KE were calculated to be 12.5U/cm2 and 34.88U/mL. respectively, Adsorption isotherm of the enzyme on the particles showed a well developed plateau of 1.3510, 4.7210, 4.4210, 8.5810U/cm2 at 30℃. To determine the specificity of chitinase for crystalline chitin, the free energy of adsorption was measured, and its was determined as about -14.62~-18.8kJ/mol.
목차
서론
재료 및 방법
균주 및 배지
효소 생성
기질제조
가수분해 반응
흡착가역성
분석
결과 및 고찰
효소의 확산- Interface mass transfer rate
효소의 흡착
효소-생성물 이동
효소반응 속도론
흡착자유에너지
요약
인용부호
첨자
참고문헌