Laccase extraction, purification and characterization from potato peels
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Date
2018
Authors
Minari, J. B.
Agho, E. E.
Journal Title
Journal ISSN
Volume Title
Publisher
Bells University Journal of Applied Sciences and Environment (BUJASE)
Abstract
Laccases are multi-copper enzymes belonging to the group of blue oxidases which oxidise diphenol and use molecular oxygen as an electron acceptor. The enzyme exists widely in plants, fungi and some bacteria. It has widespread applications in textile industries, food industries, pharmaceutical industries and bioremediation. This study was carried out to investigate the extraction, purification and characterization of laccase from potato peels. The sample was screened for laccase production by plate test method using the indicator compound Guaiacol. Extraction was carried out using submerged fermentation while ammonium sulphate was used to purify the crude enzyme. Characterization was carried out using the following parameters: pH, temperature, protein concentration, and molecular weight of the enzyme. Enzyme activity decreased with increase in pH. Activity increased from 15 oC to 25 oC and was stable from 25 oC to 45 oC and decreased afterwards from 45 oC to 65 oC. Protein concentration was high and the molecular weight of the enzyme was in the range of 36-50 kDa. Laccase activity was found to be 0.024 U/ml; optimum temperature was from 25-45 oC while optimum pH was 4.0. This study revealed that the laccase enzyme characterized from potato peels which is always found as waste materials in our environment compared favourably with laccase enzyme characterized previously from other conventional sources.
Description
Keywords
Laccase; Guaiacol; Potato peels
Citation
Minari, J. B. & Agho, E. E. (2018). Laccase extraction, purification and characterization from potato peels. Bells University Journal of Applied Sciences and Environment (BUJASE). 1(2), 1-6.