<I>Trichoderma viride</I>속 셀룰라아제에 의한 폐신문지의 효소가수분해반응의 속도론적 연구

박진원; 이승무; Kajiuchi T; Akehata T

HWAHAK KONGHAK, Vol.28, No.6, 651-658, December, 1990

Export Citation

Trichoderma viride속 셀룰라아제에 의한 폐신문지의 효소가수분해반응의 속도론적 연구

Kinetic Study on Enzymatic Hydrolysis of Wasted Newspaper by Cellulase from Trichoderma viride

박진원, 이승무, Kajiuchi T, Akehata T

초록

Trichoderma viride（IFO 30498）로부터 생성된 셀룰라아제를 이용한 폐신문지의 효소가수분해반응에 있어서 생성물인 환원당의 생성속도식에 관하여 연구하였다.
환원당의 생성속도는 생성물저해요인, 반응온도에 의한 효소의 실활과, 셀룰로오스 표면에 강하게 흡착하는 효소의 실활에 의하여 감소하였다. 셀룰로오스의 구조적 복합성을 설명할 수 있는 활성기질계수를 도입하여, 생성물저해요인과 효소가수분해 과정에서의 효소의 실활을 고려한 속도식을 연구하였다. 비 활성화된 효소의 양은 gel filtration chromatography(GFC) 법으로 분석하였다. 속도식은 폐신문지로부터 생성되는 환원당의 농도를 정확히 예측할 수 있었다.

A kinetic study of enzymatic hydrolysis of newspaper with cellulase prepared from Trichoderma viride(IFO30498)has been carried out. The rate of reducing sugar formation decelerated due to inhibition by the products, enzyme thermoinactivation, and substrate inactivation of the enzymes tightly adsorbed on the cellulose surface. The kinetics thake into account the structural complexity of cellulose which can be explanined by the activated substrate coef-ficient, the inhibition by reaction products, and the inactivation of enzyme in the course of the enzymatic hydrolysis. The inactivated enzyme quantity is measured by GFC analysis. The kinetics satisfactorily predict the reducing sugar ac-cumulation from newspaper.

[References]

Dunn NW, Gray PP, J. Ferment. Technol., 59, 419 (1981)
Tanaka M, Song GJ, Matsuno R, Appl. Microbiol. Biotechnol., 22, 13 (1985)
Jackson MA, Talburt DE, Biotechnol. Bioeng., 32, 903 (1988)
Suga K, vanDedem G, Moo-Young M, Biotechnol. Bioeng., 17, 433 (1975)
Lee SB, Biotechnol. Bioeng., 20, 141 (1978)
Okazaki M, Moo-Young M, Biotechnol. Bioeng., 20, 637 (1978)
Pettersen N, Rose EW, Biotechnol. Bioeng., 21, 997 (1979)
Ryu DDY, Biotechnol. Bioeng., 24, 1047 (1982)
Howell JA, Mangat M, Biotechnol. Bioeng., 20, 847 (1978)
Dwivedi CP, Ghose TK, J. Ferment. Technol., 57, 15 (1979)
Mandels M, Weber J, Adv. Chem. Ser., 95, 391 (1969)
Park JW, J. Chem. Eng. Jpn., 23, 4 (1990)
Shoemaker SP, Brown RD, J. Biochem. Biophys. Acta, 523, 147 (1978)
Nishzawa K, J. Ferment. Technol., 51, 267 (1973)
Shikata S, Nishizawa K, Biochemistry, 78, 499 (1978)
Miller GL, Anal. Chem., 31, 426 (1959)
Messer M, Dahlqvist A, Anal. Biochem., 14, 376 (1966)
Mandels M, Andreotti R, Roche C, Biotechnol. Bioeng., 6, 21 (1976)
Canevascini G, Gattlen C, Biotechnol. Bioeng., 23, 1573 (1981)
Ooshima H, Sakata M, Harano Y, Biotechnol. Bioeng., 28, 1727 (1986)
Castanon M, Wilke CR, Biotechnol. Bioeng., 23, 1365 (1981)

[1] Dunn NW, Gray PP, J. Ferment. Technol., 59, 419 (1981)

[2] Tanaka M, Song GJ, Matsuno R, Appl. Microbiol. Biotechnol., 22, 13 (1985)

[3] Jackson MA, Talburt DE, Biotechnol. Bioeng., 32, 903 (1988)

[4] Suga K, vanDedem G, Moo-Young M, Biotechnol. Bioeng., 17, 433 (1975)

[5] Lee SB, Biotechnol. Bioeng., 20, 141 (1978)

[6] Okazaki M, Moo-Young M, Biotechnol. Bioeng., 20, 637 (1978)

[7] Pettersen N, Rose EW, Biotechnol. Bioeng., 21, 997 (1979)

[8] Ryu DDY, Biotechnol. Bioeng., 24, 1047 (1982)

[9] Howell JA, Mangat M, Biotechnol. Bioeng., 20, 847 (1978)

[10] Dwivedi CP, Ghose TK, J. Ferment. Technol., 57, 15 (1979)

[11] Mandels M, Weber J, Adv. Chem. Ser., 95, 391 (1969)

[12] Park JW, J. Chem. Eng. Jpn., 23, 4 (1990)

[13] Shoemaker SP, Brown RD, J. Biochem. Biophys. Acta, 523, 147 (1978)

[14] Nishzawa K, J. Ferment. Technol., 51, 267 (1973)

[15] Shikata S, Nishizawa K, Biochemistry, 78, 499 (1978)

[16] Miller GL, Anal. Chem., 31, 426 (1959)

[17] Messer M, Dahlqvist A, Anal. Biochem., 14, 376 (1966)

[18] Mandels M, Andreotti R, Roche C, Biotechnol. Bioeng., 6, 21 (1976)

[19] Canevascini G, Gattlen C, Biotechnol. Bioeng., 23, 1573 (1981)

[20] Ooshima H, Sakata M, Harano Y, Biotechnol. Bioeng., 28, 1727 (1986)

[21] Castanon M, Wilke CR, Biotechnol. Bioeng., 23, 1365 (1981)