Biochemical characterization of 4-α-glucanotransferase from Saccharophagus degradans 2-40 and its potential role in glycogen degradation
Article first published online: 20 MAY 2013
© 2013 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved
FEMS Microbiology Letters
Volume 344, Issue 2, pages 145–151, July 2013
How to Cite
Hwang, S., Choi, K.-H., Kim, J. and Cha, J. (2013), Biochemical characterization of 4-α-glucanotransferase from Saccharophagus degradans 2-40 and its potential role in glycogen degradation. FEMS Microbiology Letters, 344: 145–151. doi: 10.1111/1574-6968.12167
- Issue published online: 20 JUN 2013
- Article first published online: 20 MAY 2013
- Accepted manuscript online: 29 APR 2013 10:50AM EST
- Manuscript Accepted: 25 APR 2013
- Manuscript Revised: 23 APR 2013
- Manuscript Received: 14 DEC 2012
- Marine and Extreme Genome Research Center Program of the Ministry of Land, Transportation, and Maritime Affairs
Fig. S1. SDS-PAGE (a) and molecular mass determination (b) of S. degradans MalQ. Lane 1: molecular mass marker; lane 2: cell-free extracts of pET29b without malQ; lane 3: cell-free extracts of pET29b with malQ; lane 4: purified MalQ. Molecular mass standards: ferritin (440 kDa), β-amylase (200 kDa), amyloglucosidase (97 kDa), and albumin (68 kDa).
Fig. S2. Identification of the linearized reaction products by MalQ. The reaction mixture (50 μL) containing 0.2% (w/v) maltotriose in 25 mM Tris–HCl (pH 8.5) and MalQ (1 μg) was incubated at 35 °C for 4 h. S, standard (from glucose to maltoheptaose [10 mM]); Lane 1, absence of MalQ; Lane 2, presence of MalQ; Lane 3, glucoamylase treatment (16 U, incubated at 50 °C for 8 h) after the MalQ enzyme reaction.
Table S1. Bacterial strains, plasmids, and oligonucleotides used in this study.
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