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Full-Text Articles in Biomedical Engineering and Bioengineering

Crystal Structure And Evolution Of A Prokaryotic Glucoamylase, Alexander E. Aleshin, Ping-Hua Feng, Richard B. Honzatko, Peter J. Reilly Mar 2003

Crystal Structure And Evolution Of A Prokaryotic Glucoamylase, Alexander E. Aleshin, Ping-Hua Feng, Richard B. Honzatko, Peter J. Reilly

Chemical and Biological Engineering Publications

The first crystal structures of a two-domain, prokaryotic glucoamylase were determined to high resolution from the clostridial species Thermoanaerobacterium thermosaccharolyticum with and without acarbose. The N-terminal domain has 18 antiparallel strands arranged in β-sheets of a super-β-sandwich. The C-terminal domain is an (α/α)6 barrel, lacking the peripheral subdomain of eukaryotic glucoamylases. Interdomain contacts are common to all prokaryotic Family GH15 proteins. Domains similar to those of prokaryotic glucoamylases in maltose phosphorylases (Family GH65) and glycoaminoglycan lyases (Family PL8) suggest evolution from a common ancestor. Eukaryotic glucoamylases may have evolved from prokaryotic glucoamylases by the substitution of the N-terminal ...


Beta Zeolite Supported On Silicon Carbide For Friedel–Crafts Fixed-Bed Reactions, Gauthier Wine, Joseph Matta, Jean-Philippe Tessonnier, Cuong Pham-Huu, Marc-Jacques Ledoux Jan 2003

Beta Zeolite Supported On Silicon Carbide For Friedel–Crafts Fixed-Bed Reactions, Gauthier Wine, Joseph Matta, Jean-Philippe Tessonnier, Cuong Pham-Huu, Marc-Jacques Ledoux

Jean-Philippe Tessonnier

Beta zeolite supported on silicon carbide, with high thermal conductivity and high mechanical strength, was successfully used as an active and stable catalyst for Friedel-Crafts reactions in a fixed bed configuration.


Starch‐Binding Domain Shuffling In Aspergillus Niger Glucoamylase, Catherine A.G. Cornett, Tsuei-Yun Fang, Peter J. Reilly, Clark Ford Jan 2003

Starch‐Binding Domain Shuffling In Aspergillus Niger Glucoamylase, Catherine A.G. Cornett, Tsuei-Yun Fang, Peter J. Reilly, Clark Ford

Chemical and Biological Engineering Publications

Aspergillus niger glucoamylase (GA) consists mainly of two forms, GAI [from the N‐terminus, catalytic domain + linker + starch‐binding domain (SBD)] and GAII (catalytic domain + linker). These domains were shuffled to make RGAI (SBD + linker + catalytic domain), RGAIΔL (SBD + catalytic domain) and RGAII (linker + catalytic domain), with domains defined by function rather than by tertiary structure. In addition, Paenibacillus macerans cyclomaltodextrin glucanotransferase SBD replaced the closely related A.niger GA SBD to give GAE. Soluble starch hydrolysis rates decreased as RGAII ≈ GAII ≈ GAI > RGAIΔL ≈ RGAI ≈ GAE. Insoluble starch hydrolysis rates were GAI > RGAIΔL > RGAI >> GAE ≈ RGAII > GAII, while insoluble starch ...