Zobrazeno 1 - 6
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pro vyhledávání: '"Suthipapun Tumhom"'
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Abstract Amylomaltase (AM) catalyzes transglycosylation of starch to form linear or cyclic oligosaccharides with potential applications in biotechnology and industry. In the present work, a novel AM from the mesophilic bacterium Streptococcus agalact
Externí odkaz:
https://doaj.org/article/603b3c4a035e433ca06bde6359ea7fbf
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Scientific Reports
Scientific Reports
Amylomaltase (AM) catalyzes transglycosylation of starch to form linear or cyclic oligosaccharides with potential applications in biotechnology and industry. In the present work, a novel AM from the mesophilic bacterium Streptococcus agalactiae (SaAM
Publikováno v:
World Journal of Microbiology and Biotechnology. 38
4α-Glucanotransferase (4α-GTase) is unique in its ability to form cyclic oligosaccharides, some of which are of industrial importance. Generally, low amount of enzymes is produced by or isolated from their natural sources: animals, plants, and micr
Publikováno v:
Journal of applied microbiologyReferences. 129(5)
Aim To express amylomaltase from Thermus filiformis (TfAM) in a generally recognized as safe (GRAS) organism and to use the enzyme in starch modification. Methods and results TfAM was expressed in Saccharomyces cerevisiae, using 2% (w/v) galactose in
Publikováno v:
Biochemical and Biophysical Research Communications. 488:516-521
Amylomaltase catalyzes α-1,4 glucosyl transfer reaction to yield linear or cyclic oligosaccharide products. The aim of this work is to investigate functional roles of 410s loop unique to amylomaltase from Corynebacterium glutamicum ( Cg AM). Site-di
Publikováno v:
SC30201810090027
NARO成果DBa
C30201806120001_4499.pdf
NARO成果DBa
C30201806120001_4499.pdf
Amylomaltase (AM) catalyzes inter- and intra-molecular transglycosylation reactions of glucan to yield linear and cyclic oligosaccharide products. The functional roles of the conserved histidine at position 461 in the active site of AM from Corynebac