Authors:	Berezina, OV; Zverlov, VV; Lunina, NA; Chekanovskaya, LA; Dubinina, EN; Liebl, W; Velikodvorskaya, GA
Title:	Gene and properties of thermostable 4-alpha-glucanotransferase of Thermotoga neapolitana
Source:	MOLECULAR BIOLOGY, 33: (5) 801-806 SEP-OCT 1999

Abstract:
Two clones that produced a thermostable enzyme hydrolyzing starch, amylose, and amylopectin were selected from a genome library of anaerobic extremely thermophilic bacterium Thermotoga neapolitana. The inserts of their recombinant plasmids ware sequenced. Both plasmids had the mgtA gene for maltodextrin glycosyltransferase of 442 amino acid residues. The deduced molecular weight of the enzyme, 51.9 kDa, was confirmed by SDS-PAGE. Maltodextrin glycosyltransferase (4-alpha-glucanotransferase) [EC 2.4.1.25] hydrolyzed the 1,4-alpha-glycoside bonds in oligomeric and polymeric 1,4-alpha-glucans and transferred oligosaccharides (maltotriose being the shortest one) to acceptor maltodextrins. The highest enzymic activity was observed at pH 7.0 and at 85 degrees C.

Reprints:	BEREZINA OV,RUSSIAN ACAD MED SCI,INST GENET MOL;MOSCOW 123182, RUSSIA. img@img.ras.fu
Research Institutions:	Russian Acad Med Sci, Inst Genet Mol, Moscow 123182, Russia. Univ Gottingen, Inst Microbiol & Genet, D-37077 Gottingen, Germany.