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Title: Transglycosylation properties of maltodextrin glucosidase (MalZ) from Escherichia coli and its application for synthesis of a nigerose-containing oligosaccharide

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2]; ;  [1];  [3];  [4];  [2]
  1. Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, Seoul National University, Seoul 151-921 (Korea, Republic of)
  2. Department of Biology, University of Incheon, Incheon 406-772 (Korea, Republic of)
  3. Department of Food and Biotechnology, Korea University, Jochiwon 339-700 (Korea, Republic of)
  4. Department of Biology, University of Konstanz, Konstanz 78457 (Germany)

The transglycosylation reaction of maltodextrin glucosidase (MalZ) cloned and purified from Escherichia coli K12 was characterized and applied to the synthesis of branched oligosaccharides. Purified MalZ preferentially catalyzed the hydrolysis of maltodextrin, {gamma}-cyclodextrin (CD), and cycloamylose (CA). In addition, when the enzyme was incubated with 5% maltotriose (G3), a series of transfer products were produced. The resulting major transfer products, annotated as T1, T2, and T3, were purified and their structures were determined by TLC, MALDI-TOF/MS, {sup 13}C NMR, and enzymatic analysis. T1 was identified as a novel compound, maltosyl {alpha}-1,3-maltose, whereas T2 and T3 were determined to be isopanose and maltosyl-{alpha}-1,6-maltose, respectively. These results indicated that MalZ transferred sugar moiety mainly to C-3 or C-6-OH of glucose of the acceptor molecule. To obtain highly concentrated transfer products, the enzyme was reacted with 10% liquefied cornstarch, and then glucose and maltose were removed by immobilized yeast. The T1 content of the resulting reaction mixture reached 9.0%. The mixture of T1 containing a nigerose moiety can have an immunopotentiating effect on the human body and may be a potential functional sugar stuff.

OSTI ID:
22202653
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 397, Issue 1; Other Information: Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English

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