Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (9)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Liu, H.-L.
Right arrow Articles by Reilly, P. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Liu, H.-L.
Right arrow Articles by Reilly, P. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 12, No. 2, 163-172, February 1999
© 1999 Oxford University Press

Mutations to alter Aspergillus awamori glucoamylase selectivity. IV. Combinations of Asn20->Cys/Ala27->Cys, Ser30->Pro, Gly137->Ala, 311–314 Loop, Ser411->Ala and Ser436->Pro

Hsuan-Liang Liu, Clark Ford1 and Peter J. Reilly2

1 Departments of Chemical Engineering and Food Science and Human Nutrition, Iowa State University, Ames, IA 50011, USA

Six previously constructed and nine newly constructed Aspergillus awamori glucoamylases with multiple mutations made by combining existing single mutations were tested for their ability to produce glucose from maltodextrins. Multiple mutations have cumulative effects on glucose yield, specific activity and thermostability. No general correlation between glucose yield and thermostability was observed, although mutations that presumably impede unfolding at high temperatures uniformly increase thermostability and generally increase glucose yield. Peak glucose yields decrease with increasing temperature. The best combination of high glucose yield, high specific activity and high thermostability occurs in Asn20->Cys/Ala27->Cys/Ser30->Pro/Gly137->Ala glucoamylase.

Keywords: additivity/glucoamylase/glucose yield/isomaltose/selectivity/site-directed mutagenesis

2 To whom correspondence should be addressed


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Protein Eng Des SelHome page
H.-L. Liu and W.-C. Wang
Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations
Protein Eng. Des. Sel., January 1, 2003; 16(1): 19 - 25.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
H.-L. Liu, Y. Doleyres, P. M. Coutinho, C. Ford, and P. J. Reilly
Replacement and deletion mutations in the catalytic domain and belt region of Aspergillus awamori glucoamylase to enhance thermostability
Protein Eng. Des. Sel., September 1, 2000; 13(9): 655 - 659.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.