Purification and characterisation of a novel alkalophilic alpha-D-mannosidase from Pseudomonas fluorescens
- Authors
- Park, Jae Kweon
- Issue Date
- 1-Nov-2013
- Publisher
- TAYLOR & FRANCIS LTD
- Keywords
- alpha-Mannosidase; Pseudomonas fluorescens; enzyme purification; alkalophilic; substrate specificity; algal-lytic activity
- Citation
- BIOCONTROL SCIENCE AND TECHNOLOGY, v.23, no.11, pp.1324 - 1335
- Journal Title
- BIOCONTROL SCIENCE AND TECHNOLOGY
- Volume
- 23
- Number
- 11
- Start Page
- 1324
- End Page
- 1335
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/14128
- DOI
- 10.1080/09583157.2013.838209
- ISSN
- 0958-3157
- Abstract
- An extracellular alkaline -D-mannosidase in the cell culture of a marine bacterium Pseudomonas fluorescens JK-02 was purified to homogeneity with a 30.7-fold by ammonium sulphate fractionation, anion-exchange chromatography and gel-filtration chromatography. The molecular weight of the purified enzyme was estimated to be 50.5 kDa based on the sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH and temperature of the purified enzyme were 8.5 and 30 degrees C. The K-m and V-max values of the purified enzyme towards p-nitrophenyl--D-mannopyranoside were determined to be 77 mu M and 0.23 mu M min(-1)mg(-1) of protein, respectively. The -D-mannosidase showed higher substrate specificity to -1,3-mannobiose than other isomeric substrates such as -1,2- and -1,6-mannobiose. In addition, molecular characterisation of this enzyme reveals that it belongs to a class II -mannosidase from the glycosyl hydrolase family 38. To the best of our knowledge, this is the first report on the alkalophilic -1,3 D-mannosidase of Pseudomonas species, which has selective algal-lytic activity against Alexandrium tamarense, Akashiwo sanguine, Gymnodinium catenatum, Gymnodinium mikimotoi and Prorocentrum dentatum.
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