• Title/Summary/Keyword: carboxymethylated substrate

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Manufacturing of Enzyme Immobilized Sheet Using Carboxymethylated RMP Substrate (카르복시메틸화 RMP를 이용한 효소 고정화시트의 제조)

  • 조남석
    • Journal of Korea Technical Association of The Pulp and Paper Industry
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    • v.35 no.2
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    • pp.39-45
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    • 2003
  • This study was performed to develop the new type enzyme immobilization sheet from carboxymethylated refiner mechanical pulp (CRMP) substrate. Enzyme immobilization was attempted to couple carboxyl groups of CRMP with amino groups of the enzyme, trypsin, through the reaction of carbodiimide reagent, 1-ethyl-3-(3-dimethyl aminopropyl)-carbodimide (EDC ). Immobilization carrier, water insoluble CRMP fraction (CRMP-IS), was successfully reacted with the enzyme, formed peptide linkage like -CONH- at 1680$cm^{-1}$ / and new ester linkage like -COO$CH_3$, methylester at 1735$cm^{-1}$ /, and produced enzyme immobilized substrate (CRMP-IST). The enzyme immobilized handsheet was prepared by mixing the above chelated enzyme immobilized substrate(CRMP-IST) with kraft pulp by paper sheet machine like papermaking process. The sheet weight and strength were increased with increasing dosage of CRMP-IST, and decreased at more than 10% mixing of CRMP-IST, but higher than the controls. Concerning activities of immobilized trypsin(CRMP-IST) sheet by caseinolysis, the teared-off sheet with shaking was shown higher enzyme activities than sheet shape without shaking. In conclusion, this enzyme immobilized sheet would be expected easy handling for practical application and reutilization.

Characteristics of Carbozymethylated Substrates from Delignified Autohydrolyzed Substrates (탈리그닌한 자기가수분해 시료로부터 준비한 카복시메틸화 시료의 특성)

  • Cho, Nam-Seok
    • Journal of the Korean Wood Science and Technology
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    • v.32 no.1
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    • pp.28-34
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    • 2004
  • This study was performed to evaluate the characteristics of the carboxymethylated substrate from high reactive autohydrolyzed cellulose (HRC) and those of commercial α-cellulose (CAC) and refiner mechanical pulp (RMP). Saccharification rates of HRC substrate were achieved over 70% with 12 hr hydrolysis, about 90% with 24 hr, and 99.5% with 72 hr. CMCase and avicelase activities of cellulase onozuka were 4.09 ㎛ G/mg·min and 14.0 ㎛ G/mg·min, respectively. There were no any significant changes in cellulase activities with this substrate. The saccharification rates of CAC and RMP were very low, 57% and 38% with 72 hr, respectively. Those lignin-zero autohydrolyzed substrates, HRC and CAC, were highly carboxymethylated at the high alkali concentration, near 30%, for 3 hr. reaction, and resulted in 1.13-1.15 of D.S., besides 0.85 of D.S. from RMP. Water solubilities of carboxymethylated substrates were increased with an increase of D.S., 98-98.5% from HRC and CAC and 31.5% from RMP. RMP which has low specific surface area showed lower water retention values, compared to high values of 435 and 321% from CAC and HRC, respectively. There were no direct relationship between surface area and swelling ratio of the substrates.