Enhanced maltose production through mutagenesis of acceptor binding subsite +2 in Bacillus stearothermophilus maltogenic amylase

Journal of Biotechnology

Volumn 217, Issue , 2016, Pages 53-61

  Sun, Yecheng ^a   Duan, Xuguo ^a   Wang, Lei ^a   Wu, Jing ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

Bacillus stearothermophilus; High maltose syrup; Maltogenic amylase; Transglycosylation

Indexed keywords

AMYLASES; BACTERIOLOGY; ENZYMES; GLYCOSYLATION; HYDROPHILICITY; MUTAGENESIS; OLIGOSACCHARIDES;

BACILLUS STEAROTHERMOPHILUS; BACILLUS STEAROTHERMOPHILUS MALTOGENIC AMYLASE; HIGH MALTOSE SYRUP; INDUSTRIAL CONDITIONS; MALTOGENIC AMYLASE; SITE DIRECTED MUTAGENESIS; TRANS GLYCOSYLATION ACTIVITY; TRANSGLYCOSYLATION;

MALTOSE;

AMYLASE; MALTOGENIC AMYLASE; MALTOSE; MALTOTRIOSE; UNCLASSIFIED DRUG; ACARBOSE; BACTERIAL DNA; GLUCAN 1,4-ALPHA-MALTOHYDROLASE; GLUCOSE; GLYCOSIDASE; STARCH; TRISACCHARIDE;

ARTICLE; CONTROLLED STUDY; GEOBACILLUS STEAROTHERMOPHILUS; GLYCOSYLATION; HYDROLYSIS; HYDROPHILICITY; NONHUMAN; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; TEMPERATURE; THERMOSTABILITY; BACTERIAL GENE; BINDING SITE; BIOSYNTHESIS; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR MODEL;

ACARBOSE; AMYLASES; BINDING SITES; CLONING, MOLECULAR; DNA, BACTERIAL; ESCHERICHIA COLI; GENES, BACTERIAL; GEOBACILLUS STEAROTHERMOPHILUS; GLUCOSE; GLYCOSIDE HYDROLASES; GLYCOSYLATION; HYDROLYSIS; MALTOSE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; STARCH; SUBSTRATE SPECIFICITY; TRISACCHARIDES;

EID: 84947966674     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2015.11.007     Document Type: Article

References (25)

1. Anon. Maltogenase Novo Nordisk product sheet, (1990).
2. Anon. Maltogenic amylase from Bacillus stearothermophilus expressed in Bacillus subtilis. Food and Agriculture Organization of the United Nations, (1999).
3. Beier L., Svendsen A., Andersen C., Frandsen T.P., Borchert T.V., Cherry J.R. Conversion of the maltogenic alpha-amylase novamyl into a CGTase. Protein Eng. 2000, 13(7):509-513.
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72(1-2):248-254.
5. Cha H.J., Yoon H.G., Kim Y.W., Lee H.S., Kim J.W., Kweon K.S., Oh B.H., Park K.H. Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose. Eur. J. Biochem. 1998, 253(1):251-262.
6. Cheng J., Wu D., Chen S., Chen J., Wu J. High-level extracellular production of γ-cyclodextrin glycosyltransferase with recombinant E. coli bl21 (de3). J. Agric. Food Chem. 2011, 59:3797-3802.
7. Dauter Z., Dauter M., Brzozowski A.M., Christensen S., Borchert T.V., Beier L., Wilson K.S., Davies G.J. X-ray structure of novamyl, the five-domain maltogenic alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7 angstrom resolution. Biochemistry 1999, 38(26):8385-8392.
8. Duan X., Chen J., Wu J. Optimization of pullulanase production in E. coli by regulation of process conditions and supplement with natural osmolytes. Bioresour. Technol. 2013, 146:379-385.
9. Gaouar O., Aymard C., Zakhia N., Rios G.M. Enzymatic hydrolysis of cassava starch into maltose syrup in a continuous membrane reactor. J. Chem. Technol. Biotechnol. 1997, 69(3):367-375.
10. Gaouar O., Zakhia N., Aymard C., Rios G.M. Production of maltose syrup by bioconversion of cassava starch in an ultrafiltration reactor. Ind. Crops Prod. 1998, 7(2-3):159-167.
11. Guzmanmaldonado H., Paredeslopez O. Amylolytic enzymes and products derived from starch-a review. Crit. Rev. Food Sci. 1995, 35(5):373-403. arxiv:/www.idtdna.com/CodonOpt.
12. Lee S.J., Kim J.C., Kim M.J., Kitaoka M., Park C.S., Lee S.Y., Ra M.J., Moon T.W., Robyt J.F., Park K.H. Transglycosylation of naringin by Bacillus stearothermophilus maltogenic amylase to give glycosylated naringin. J. Agric. Food Chem. 1999, 47(9):3669-3674.
13. Leemhuis H., Dijkstra B.W., Dijkhuizen L. Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase. FEBS Lett. 2002, 514(2-3):189-192.
14. Leemhuis H., Rozeboom H.J., Wilbrink M., Euverink G.J.W., Dijkstra B.W., Dijkhuizen L. Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1. Biochemistry 2003, 42(24):7518-7526.
15. Muraki M., Harata K., Jigami Y. Dissection of the functional-role of structural elements of tyrosine-63 in the catalytic action of human lysozyme. Biochemistry 1992, 31(38):9212-9219.
16. Nakamura A., Haga K., Yamane K. Four aromatic residues in the active-center of cyclodextrin glucanotransferase from alkalophilic Bacillus -sp-1011- effects of replacements on substrate-binding and cyclization characteristics. Biochemistry 1994, 33(33):9929-9936.
17. Nebesny E. Changes of carbohydrates and molecular structure of dextrins during enzymatic hydrolysis of starch with maltogenase participation. Starch 1990, 42(11):432-436.
18. Outtrap H., Norman B.E. Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-dna techniques. Starch 1984, 36(12):405-411.
19. Park K.H., Kim M.J., Lee H.S., Han N.S., Kim D., Robyt J.F. Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors. Carbohydr. Res. 1998, 313(3-4):235-246.
20. Parsiegla G., Schmidt A.K., Schulz G.E. Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production. Eur. J. Biochem. 1998, 255(3):710-717.
21. Saha B.C., Zeikus J.G. Improved method for preparing high maltose conversion syrups. Biotechnol. Bioeng. 1989, 34(3):299-303.
22. Spurlino J.C., Lu G.Y., Quiocho F.A. The 2.3-a resolution structure of the maltose-binding or maltodextrin-binding protein, a primary receptor of bacterial active-transport and chemotaxis. J. Biol. Chem. 1991, 266(8):5202-5219.
23. Svensson B. Protein engineering in the alpha-amylase family-catalytic mechanism, substrate-specificity, and stability. Plant Mol. Biol. 1994, 25(2):141-157.
24. Uitdehaag J.C., Mosi R., Kalk K.H., van der Veen B.A., Dijkhuizen L., Withers S.G., Dijkstra B.W. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Nat. Struct. Biol. 1999, 6(5):432-436.
25. van der Veen B.A., Leemhuis H., Kralj S., Uitdehaag J.C.M., Dijkstra B.W., Dijkhuizen L. Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase. J. Biol. Chem. 2001, 276(48):44557-44562.