Applied Microbiology and Biotechnology

, Volume 65, Issue 3, pp 273–280

Isolation and characterization of a novel intracellular glucosyltransferase from the acarbose producer Actinoplanes sp. CKD485-16

Biotechnologically Relevant Enzymes and Proteins

DOI: 10.1007/s00253-004-1639-x

Cite this article as:
Choi, B.T. & Shin, C.S. Appl Microbiol Biotechnol (2004) 65: 273. doi:10.1007/s00253-004-1639-x


A novel intracellular glucosyltransferase (GTase) was isolated from cells of Actinoplanes sp. CKD485-16—acarbose-producing cells. The enzyme was purified by DEAE-cellulose and G75-40 Sephadex chromatography. The molecular mass of the enzyme was estimated to be 62 kDa by SDS-polyacrylamide gel electrophoresis, and its isoelectric point (pI) was pH 4.3. The N-terminal sequence of the GTase consisted of NH2-Ser-Val-Pro-Leu-Ser-Leu-Pro-Ala-Glu-Trp. The optimum pH and temperature were 7.5 and 30°C. The enzyme was stable in a pH range of 5.5–9.0 and below 40°C. Enzymatic reactions were performed by incubating the GTase with various substrates. The GTase converted acarbose into component C, maltose into trehalose, and maltooligosaccharides into maltooligosyl trehaloses. The reactions were reversible. Various acarbose analogs were tested as inhibitors against the GTase as a means to suppress component C formation. Valienamine was the most potent, with an IC50 value of 2.4×10−3 mM and showed a competitive inhibition mode.

Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  1. 1.Department of Biotechnology, College of EngineeringYonsei UniversitySeoulSouth Korea

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