Glucoamylase produced by Rhizopus and by a recombinant yeast containing the Rhizopus glucoamylase gene.
نویسندگان
چکیده
منابع مشابه
Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path.
GA (glucoamylase) hydrolyses starch and polysaccharides to beta-D-glucose. RoGA (Rhizopus oryzae GA) consists of two functional domains, an N-terminal SBD (starch-binding domain) and a C-terminal catalytic domain, which are connected by an O-glycosylated linker. In the present study, the crystal structures of the SBD from RoGA (RoGACBM21) and the complexes with beta-cyclodextrin (SBD-betaCD) an...
متن کاملThe Rhizopus niveus glucoamylase-catalyzed reaction for substrate maltose in the absence or presence of acetonitrile
In the presence or absence of acetonitrile CH3CN, the molecular mechanism on the Rhizopus niveus glucoamylse (GA)-catalyzed reaction was studied by the steady-state kinetics for a substrate maltose (G2). At high concentration of G2, the GA-catalyzed reaction was observed not to obey the Michaelis kinetics and was reasonably explained with a mechanism of the substrate-inhibition involving the te...
متن کاملSolution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase.
CBMs (carbohydrate-binding modules) function independently to assist carbohydrate-active enzymes. Family 21 CBMs contain approx. 100 amino acid residues, and some members have starchbinding functions or glycogen-binding activities. We report here the first structure of a family 21 CBM from the SBD (starch-binding domain) of Rhizopus oryzae glucoamylase (RoCBM21) determined by NMR spectroscopy. ...
متن کاملEfficient and direct fermentation of starch to ethanol by sake yeast strains displaying fungal glucoamylases.
Aspergillus oryzae glucoamylases encoded by glaA and glaB, and Rhizopus oryzae glucoamylase, were displayed on the cell surface of sake yeast Saccharomyces cerevisiae GRI-117-UK and laboratory yeast S. cerevisiae MT8-1. Among constructed transformants, GRI-117-UK/pUDGAA, displaying glaA glucoamylase, produced the most ethanol from liquefied starch, although MT8-1/pUDGAR, displaying R. oryzae gl...
متن کاملExtraction and Purification of Glucoamylase and Protease Produced by Aspergillus awamori in a Single-Stage Fermentation
Simultaneous extraction and purification of glucoamylase and protease produced concomitantly by Aspergillus awamori Nakazawa MTCC 6652 in a single fermentor using solid-state fermentation (SSF) has been studied. Soaking for 2 h at room temperature (around 30 °C) in 10 % glycerol was found to be most suitable for optimum simultaneous extraction of glucoamylase and protease with the yield of 8645...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1986
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.50.1737