Article
Mutations of barley beta-amylase that improve substrate-binding affinity and thermostability.
Molecular genetics and genomics : MGG - 1 Nov 2001
Ma Y F, Evans D E, Logue S J, Langridge P
Abstract excerpt
Three allelic forms of barley beta-amylase (Sd1, Sd2H and Sd2L) exhibit different thermostability and kinetic properties. These differences critically influence the malting quality of barley varieties. To understand the molecular basis for the different properties of these three allelic forms, Sd1 and Sd2L beta-amylase cDNAs were cloned, and the effects of the amino acid substitutions between them were evaluated...
Topics
- Alleles
- Amino Acid Substitution
- Base Sequence
- DNA Primers
- DNA, Complementary
- Electrophoresis, Polyacrylamide Gel
- Enzyme Stability
- Escherichia coli
- Hordeum
- Molecular Sequence Data
- Mutagenesis, Site-Directed