Purification and characterization of a novel transfructosylating enzyme from Bacillus macerans EG-6
- Authors
- Park, Jong-Pil; Oh, Tae-Kwang; Yun, Jong-Won
- Issue Date
- Dec-2001
- Keywords
- Bacillus macerans EG-6; Fructo-oligosaccharide; Purification; Transfructosylating enzyme
- Citation
- Process Biochemistry, v.37, no.5, pp 471 - 476
- Pages
- 6
- Journal Title
- Process Biochemistry
- Volume
- 37
- Number
- 5
- Start Page
- 471
- End Page
- 476
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/75277
- DOI
- 10.1016/S0032-9592(01)00237-0
- ISSN
- 1359-5113
1873-3298
- Abstract
- A novel transfructosylating enzyme, which produces fructo-oligosaccharides from sucrose from Bacillus macerans EG-6 were purified 63.5-fold by ammonium sulphate precipitation (20-60%), CM-Sepharose CL 6B and fast protein liquid chromatographies on Resource Q, Phenyl-Superose HR 5/5 and Mono S (Pharmacia, Uppsala, Sweden). The minimum molecular mass of the purified enzyme was 66 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was stable at the pH range of 5.0-7.0 and had an optimum pH at 5.0. The optimum temperature for enzyme activity was at 50°C. The oligosaccharide compositions in reaction products were significantly different on using the enzyme obtained from each purification step. For example, crude enzyme unusually produced selectively GF5- and GF6-fructo-oligosaccharide whereas purified enzyme produced mainly 1-kestose (GF2) and nystose (GF3) as in the case of other transfructosylating enzymes. © 2001 Elsevier Science Ltd. All rights reserved.
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