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섬유소분해효소에 의한 중규모 고급폐지재생 탈묵공정
Mid-Scale Deinking Process for Office Waste Paper Recycling using Cellulase
인하대학교 공과대학 생물공학과, 인천 402-751 1울산대학교 공과대학 화학공학과, 울산 680-749
Department of Biological Engineering, Inha University, Inchon 402-751, Korea 1Department of Chemical Engineering, Ulsan University, Ulsan 680-749, Korea
HWAHAK KONGHAK, June 2000, 38(3), 434-439(6), NONE
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Abstract
Trichoderma reesei Rut C-30에서 생산된 crude cellulase와 이를 다시 단백질 분해효소의 일종인 papain으로 부분 가수분해한 cellulase를 이용하여 고급폐지의 중규모 탈묵공정을 수행하였다. 이 탈묵공정의 결과를 상업용 탈묵효소인 Novozym 342를 이용하는 효소적 탈묵공정과 가성소다를 사용하는 전통 화학적 탈묵공정과 비교하였다. 중규모 탈묵공정에서 crude cellulase 농도에 따른 탈묵효율은 CMCase activity 기준 3units/g Oven Paper에서 백색도 (brightness)와 여수도(freeness)가 최대갑을 보였다. 소규모에 비해 물리적 강도와 백색도가 높았으나 여수도와 수율은 낮았다. 중규모의 경우 3 units에서 백색도와 여수도에서 최적인 반면, 소규모의 경우는 2 units의 경우가 최적임을 보였다. Papain 처리된 효소에 의한 탈묵은 Novozym 342와 비슷한 결과를 보였고, 가성소다를 사용하는 기존의 탈묵공정에 비해서는 백색도와 여수도는 우수하였으나 물리적 강도에서는 다소 낮았고, 수율면에서도 낮은 결과를 나타냈다. 본 실험에서 Trichoderma reesei Rut C-30에 의해 생산된 curde cellulase를 papin으로 처리한 효소의 endo 성분과 exo 성분의 조합비율이 상업적으로 생산되는 탈묵효소(Novozym 342)와 비슷하게 나타났으며, 이는 경제성 있는 탈묵용 효소로서의 가능성을 보여주었다.
Enzymatic deinking of office-waste paper was studied using crude cellulase and papain-hydrolyzed cellulase from Trichoderma Rut C-30 in small-scale and mid-scale. The results were compared with deinkings using commercial enzyme(Novozym 342) and conventional chemical methods. Maximum brightness and freeness were obtained at 3 units/g Oven Dry Paper(ODP) of CMCase activity using crude cellulase in mid-scale deinking experiments. The deinked pulp had higher physical strength and brightness, and lower freeness and yield than the pulp deinked in small scale. In small scale deinking, maximum brightness and freeness were obtained at 2 units/g ODP. Deinking by papain-hydrolyzed cellulase showed similar results with those by Novozym 342. It was better in brightness and freensess, but showed lower physical strength and yield, than the conventional deinking by sodium hydroxide. The ration of endo-1,4-glucanase and exo-1,4-glucanase components in papain-hydrolyzed cellulase from Trichoderma reesei Rut-30 was similar to that of commercial enzyme, Novozym 342, implicating a successful application as a deinking enzyme.
References
Kirk TK, Jeffries TW, "Roles for Microbial Enzymes in Pulp and Paper Processing," ACS Symp. Ser. 655, ACS, Washington DC, 2 (1996)
Bajpai P, Bajpai PK, TAPPI J., 81(12), 111 (1998)
Jeffries TW, Klungness JH, Sykes MS, Rutledge-Cropsey KR, TAPPI J., 77(4), 173 (1994)
Kim TJ, Ow SSK, Eom TJ, "Tappi Pulping Conference Proceedings," TAPPI PRESS, Atlanta, 1023 (1991)
Heise OU, Uniwin JP, Klungness JH, Fineran WG, Sykes M, Abubakr S, TAPPI J., 79(3), 207 (1996)
Tomme PH, van Tilbeurgh G, van Damme JP, van de Kerckhove J, Knowles J, Teeri T, Claeyssens M, Eur. J. Biochem., 170, 57 (1998)
Putz HJ, Renner K, Gottsching L, Jokinen O, "Tappi Pulping Conference Proceedings," TAPPI PRESS, Atlanta, 877 (1994)
Heindel TJ, TAPPI J., 82(31), 115 (1998)
Fan LT, Gharpuray MM, Lee YH, "Cellulose Hydrolysis," Springer-Verlag, Berlin Heidelberg, 21 (1987)
Klyosov AA, Biochem., 29(47), 10577 (1990)
Kim DW, Chung YK, Jang YH, Shon KH, Korean J. Biotech. Bioeng., 11(6), 718 (1996)
Kim BH, Jun Y, J. Korean Tappi, 26(2), 23 (1994)
Sarkar JM, Cosper DR, Hartig EJ, TAPPI J., 78(2), 89 (1995)
Ryu KG, Bae JS, Lee SM, Koo YM, Theor. Appl. Chem. Eng., 5(2), 3165 (1999)
Stork G, Pereira H, Wood TM, Dusterhoft EM, Toft A, Puls J, TAPPI J., 78(2), 79 (1995)
Wood TM, Bhat KM, "Methods for Measuring Cellulase Activities,"Methods of Enzymology 160, Academic Press Inc., New York, 87 (1988)
Han WS, Koo YM, HWAHAK KONGHAK, 36(5), 759 (1998)
Bajpai P, Bajpai PK, TAPPI J., 81(12), 111 (1998)
Jeffries TW, Klungness JH, Sykes MS, Rutledge-Cropsey KR, TAPPI J., 77(4), 173 (1994)
Kim TJ, Ow SSK, Eom TJ, "Tappi Pulping Conference Proceedings," TAPPI PRESS, Atlanta, 1023 (1991)
Heise OU, Uniwin JP, Klungness JH, Fineran WG, Sykes M, Abubakr S, TAPPI J., 79(3), 207 (1996)
Tomme PH, van Tilbeurgh G, van Damme JP, van de Kerckhove J, Knowles J, Teeri T, Claeyssens M, Eur. J. Biochem., 170, 57 (1998)
Putz HJ, Renner K, Gottsching L, Jokinen O, "Tappi Pulping Conference Proceedings," TAPPI PRESS, Atlanta, 877 (1994)
Heindel TJ, TAPPI J., 82(31), 115 (1998)
Fan LT, Gharpuray MM, Lee YH, "Cellulose Hydrolysis," Springer-Verlag, Berlin Heidelberg, 21 (1987)
Klyosov AA, Biochem., 29(47), 10577 (1990)
Kim DW, Chung YK, Jang YH, Shon KH, Korean J. Biotech. Bioeng., 11(6), 718 (1996)
Kim BH, Jun Y, J. Korean Tappi, 26(2), 23 (1994)
Sarkar JM, Cosper DR, Hartig EJ, TAPPI J., 78(2), 89 (1995)
Ryu KG, Bae JS, Lee SM, Koo YM, Theor. Appl. Chem. Eng., 5(2), 3165 (1999)
Stork G, Pereira H, Wood TM, Dusterhoft EM, Toft A, Puls J, TAPPI J., 78(2), 79 (1995)
Wood TM, Bhat KM, "Methods for Measuring Cellulase Activities,"Methods of Enzymology 160, Academic Press Inc., New York, 87 (1988)
Han WS, Koo YM, HWAHAK KONGHAK, 36(5), 759 (1998)