Effects of organic solvents on the activity of free and immobilised laccase from Rhus vernicifera
Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use evaluated, using either N, N-dimethyl- p-phenylenediamine or 2,6-dimethoxyphenol as substrate. Immobilisation greatly enhanced enzyme thermostabil...
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Published in | International journal of biological macromolecules Vol. 47; no. 4; pp. 488 - 495 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier B.V
01.11.2010
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Abstract | Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use evaluated, using either
N,
N-dimethyl-
p-phenylenediamine or 2,6-dimethoxyphenol as substrate. Immobilisation greatly enhanced enzyme thermostability, resulted in negligible loss of activity, and showed excellent re-use potential, with >80% relative activity retained after 15
cycles in aqueous solvent. Immobilised
Rhus laccase (I-RL) was more catalytically active in both hydrophobic and hydrophilic organic solvents than free RL. With water-immiscible organic solvents, both free RL and I-RL required a minimum water content to achieve activity. With water-miscible organic solvents, in general a water content of ∼20–50% (v/v) was required to achieve activity using free RL, whereas with I-RL less water was generally required to achieve enzyme activity, and therefore considerably higher relative activity was exhibited at lower water contents. Kinetic investigations showed that the rate of substrate disappearance generally followed a pseudo-first-order law, and for evaluated water-immiscible organic solvents rate constants generally increased with decrease of hydrophobicity, however, in water-miscible organic solvents no such relationship was observed. Some discussion of the potential interactions between organic solvent molecules and enzyme active centres was provided to explain obtained results. |
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AbstractList | Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use evaluated, using either N,N-dimethyl-p-phenylenediamine or 2,6-dimethoxyphenol as substrate. Immobilisation greatly enhanced enzyme thermostability, resulted in negligible loss of activity, and showed excellent re-use potential, with >80% relative activity retained after 15 cycles in aqueous solvent. Immobilised Rhus laccase (I-RL) was more catalytically active in both hydrophobic and hydrophilic organic solvents than free RL. With water-immiscible organic solvents, both free RL and I-RL required a minimum water content to achieve activity. With water-miscible organic solvents, in general a water content of [inline image]20-50% (v/v) was required to achieve activity using free RL, whereas with I-RL less water was generally required to achieve enzyme activity, and therefore considerably higher relative activity was exhibited at lower water contents. Kinetic investigations showed that the rate of substrate disappearance generally followed a pseudo-first-order law, and for evaluated water-immiscible organic solvents rate constants generally increased with decrease of hydrophobicity, however, in water-miscible organic solvents no such relationship was observed. Some discussion of the potential interactions between organic solvent molecules and enzyme active centres was provided to explain obtained results. Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use evaluated, using either N,N-dimethyl-p-phenylenediamine or 2,6-dimethoxyphenol as substrate. Immobilisation greatly enhanced enzyme thermostability, resulted in negligible loss of activity, and showed excellent re-use potential, with >80% relative activity retained after 15 cycles in aqueous solvent. Immobilised Rhus laccase (I-RL) was more catalytically active in both hydrophobic and hydrophilic organic solvents than free RL. With water-immiscible organic solvents, both free RL and I-RL required a minimum water content to achieve activity. With water-miscible organic solvents, in general a water content of ∼20-50% (v/v) was required to achieve activity using free RL, whereas with I-RL less water was generally required to achieve enzyme activity, and therefore considerably higher relative activity was exhibited at lower water contents. Kinetic investigations showed that the rate of substrate disappearance generally followed a pseudo-first-order law, and for evaluated water-immiscible organic solvents rate constants generally increased with decrease of hydrophobicity, however, in water-miscible organic solvents no such relationship was observed. Some discussion of the potential interactions between organic solvent molecules and enzyme active centres was provided to explain obtained results. Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use evaluated, using either N,N-dimethyl-p-phenylenediamine or 2,6-dimethoxyphenol as substrate. Immobilisation greatly enhanced enzyme thermostability, resulted in negligible loss of activity, and showed excellent re-use potential, with >80% relative activity retained after 15 cycles in aqueous solvent. Immobilised Rhus laccase (I-RL) was more catalytically active in both hydrophobic and hydrophilic organic solvents than free RL. With water-immiscible organic solvents, both free RL and I-RL required a minimum water content to achieve activity. With water-miscible organic solvents, in general a water content of ∼20-50% (v/v) was required to achieve activity using free RL, whereas with I-RL less water was generally required to achieve enzyme activity, and therefore considerably higher relative activity was exhibited at lower water contents. Kinetic investigations showed that the rate of substrate disappearance generally followed a pseudo-first-order law, and for evaluated water-immiscible organic solvents rate constants generally increased with decrease of hydrophobicity, however, in water-miscible organic solvents no such relationship was observed. Some discussion of the potential interactions between organic solvent molecules and enzyme active centres was provided to explain obtained results. Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use evaluated, using either N, N-dimethyl- p-phenylenediamine or 2,6-dimethoxyphenol as substrate. Immobilisation greatly enhanced enzyme thermostability, resulted in negligible loss of activity, and showed excellent re-use potential, with >80% relative activity retained after 15 cycles in aqueous solvent. Immobilised Rhus laccase (I-RL) was more catalytically active in both hydrophobic and hydrophilic organic solvents than free RL. With water-immiscible organic solvents, both free RL and I-RL required a minimum water content to achieve activity. With water-miscible organic solvents, in general a water content of ∼20–50% (v/v) was required to achieve activity using free RL, whereas with I-RL less water was generally required to achieve enzyme activity, and therefore considerably higher relative activity was exhibited at lower water contents. Kinetic investigations showed that the rate of substrate disappearance generally followed a pseudo-first-order law, and for evaluated water-immiscible organic solvents rate constants generally increased with decrease of hydrophobicity, however, in water-miscible organic solvents no such relationship was observed. Some discussion of the potential interactions between organic solvent molecules and enzyme active centres was provided to explain obtained results. |
Author | Lu, Rong Wan, Yun-Yang Miyakoshi, Tetsuo Xiao, Ling Chen, Chen-Loung Kennedy, John F. Knill, Charles J. Du, Yu-Min |
Author_xml | – sequence: 1 givenname: Yun-Yang surname: Wan fullname: Wan, Yun-Yang organization: College of Resource and Environmental Science, Wuhan University, Wuhan 430072, Hubei, China – sequence: 2 givenname: Rong surname: Lu fullname: Lu, Rong organization: Department of Industrial Chemistry, Meiji University, Higashi-mita, Tama-ku, Kawasaki 214, Japan – sequence: 3 givenname: Ling surname: Xiao fullname: Xiao, Ling organization: College of Resource and Environmental Science, Wuhan University, Wuhan 430072, Hubei, China – sequence: 4 givenname: Yu-Min surname: Du fullname: Du, Yu-Min organization: College of Resource and Environmental Science, Wuhan University, Wuhan 430072, Hubei, China – sequence: 5 givenname: Tetsuo surname: Miyakoshi fullname: Miyakoshi, Tetsuo organization: Department of Industrial Chemistry, Meiji University, Higashi-mita, Tama-ku, Kawasaki 214, Japan – sequence: 6 givenname: Chen-Loung surname: Chen fullname: Chen, Chen-Loung organization: Department of Wood and Paper Science, North Carolina State University, Raleigh, NC 27695-8005, USA – sequence: 7 givenname: Charles J. surname: Knill fullname: Knill, Charles J. organization: Chembiotech Laboratories, Institute of Advanced Science & Technology, 5, The Croft, Buntsford Drive Stoke Heath, Bromsgrove, Worcestershire B60 4JE, UK – sequence: 8 givenname: John F. surname: Kennedy fullname: Kennedy, John F. email: jfk@chembiotech.co.uk organization: Chembiotech Laboratories, Institute of Advanced Science & Technology, 5, The Croft, Buntsford Drive Stoke Heath, Bromsgrove, Worcestershire B60 4JE, UK |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20647020$$D View this record in MEDLINE/PubMed |
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Keywords | Chitosan Catalysis Hydrophobicity Enzyme Rhus laccase Immobilisation |
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Snippet | Rhus laccase (RL) was covalently immobilised onto chitosan, and the effects of immobilisation on pH optimum, enzyme activity, thermostability, and re-use... |
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SubjectTerms | Biocatalysis - drug effects Catalysis Chitosan Enzyme Enzyme Stability - drug effects Enzymes Enzymes, Immobilized - metabolism Hydrogen-Ion Concentration - drug effects Hydrophobicity Immobilisation Kinetics Laccase - metabolism Organic Chemicals - pharmacology Oxidation-Reduction - drug effects Rhus Rhus - enzymology Rhus laccase Solvents - pharmacology Temperature Water |
Title | Effects of organic solvents on the activity of free and immobilised laccase from Rhus vernicifera |
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