TY - JOUR
T1 - Effect of chain length on the activity of free and immobilized alcohol dehydrogenase towards aliphatic alcohols
AU - Cea, Glenda
AU - Wilson, Lorena
AU - Bolívar, Juan Manuel
AU - Markovits, Andrés
AU - Illanes, Andrés
N1 - Funding Information:
This work was funded by FONDEF Grant D04I1007, CSIC (Spain)-CONICYT (Chile) Grant 177-2007 and Spanish CICYT Project CTQ2005-02420 /PPQ.
PY - 2009/3/5
Y1 - 2009/3/5
N2 - As long-chain alcohol dehydrogenases are not easily available and seldom reported enzymes, it is worthwhile to appraise the potential of well known dehydrogenases, like horse liver alcohol dehydrogenases (HLAD), for the oxidation of long-chain aliphatic alcohols. Oxidation of docosanol (C22) and tetracosanol (C24) is of technological relevance within an industrial platform for the fractionation and upgrading of tall-oil from the Kraft pulping process. Results are presented on the characterization of free and immobilized HLAD with respect to their potential for oxidizing long-chain aliphatic alcohols. Enzyme activity with respect to chain length and pH is presented. Activity for both free and immobilized HLAD increased with pH up to 8.8, but behavior with respect to chain length varied from one biocatalyst to the other. Even though both biocatalysts were less active towards very long-chain aliphatic alcohols, immobilized HLAD had an activity on docosanol and tetracosanol higher than 50% of the value obtained with ethanol, butanol and octanol, which is encouraging and has not been previously reported. Investigation on thermophilic sources and further immobilization strategies are underway to obtain more active and stable catalysts amenable for working at high temperatures which is quite relevant in this case due to the poor solubility of substrates.
AB - As long-chain alcohol dehydrogenases are not easily available and seldom reported enzymes, it is worthwhile to appraise the potential of well known dehydrogenases, like horse liver alcohol dehydrogenases (HLAD), for the oxidation of long-chain aliphatic alcohols. Oxidation of docosanol (C22) and tetracosanol (C24) is of technological relevance within an industrial platform for the fractionation and upgrading of tall-oil from the Kraft pulping process. Results are presented on the characterization of free and immobilized HLAD with respect to their potential for oxidizing long-chain aliphatic alcohols. Enzyme activity with respect to chain length and pH is presented. Activity for both free and immobilized HLAD increased with pH up to 8.8, but behavior with respect to chain length varied from one biocatalyst to the other. Even though both biocatalysts were less active towards very long-chain aliphatic alcohols, immobilized HLAD had an activity on docosanol and tetracosanol higher than 50% of the value obtained with ethanol, butanol and octanol, which is encouraging and has not been previously reported. Investigation on thermophilic sources and further immobilization strategies are underway to obtain more active and stable catalysts amenable for working at high temperatures which is quite relevant in this case due to the poor solubility of substrates.
KW - Alcohol dehydrogenase
KW - Immobilized enzyme
KW - Long-chain fatty acids
KW - Polycosanols
UR - http://www.scopus.com/inward/record.url?scp=58149305792&partnerID=8YFLogxK
U2 - 10.1016/j.enzmictec.2008.10.021
DO - 10.1016/j.enzmictec.2008.10.021
M3 - Article
AN - SCOPUS:58149305792
SN - 0141-0229
VL - 44
SP - 135
EP - 138
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
IS - 3
ER -