AI Article Synopsis
- Random mutagenesis on beta-agarase from Zobellia galactanivorans led to the creation of three mutant enzymes (E99K, T307I, E99K-T307I) with significantly improved catalytic activity, achieving up to 200% the activity of the wild type at 40°C.
- All three mutants demonstrated stability at temperatures up to 50°C, with E99K-T307I showing the highest thermostability and a melting temperature increase of 5.2°C compared to the wild-type enzyme.
- The presence of 1 mM CaCl2 enhanced the activity and thermostability of both the wild-type and E99K-T307I enzymes, with the latter achieving an impressive
Article Abstract
Random mutagenesis was performed on beta-agarase, AgaB, from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutants E99K, T307I and E99K-T307I were approx. 140, 190 and 200%, respectively, of wild type beta-agarase (661 U/mg) at 40 degrees C. All three mutant enzymes were stable up to 50 degrees C and E99K-T307I had the highest thermostability. The melting temperature (Tm) of E99K-T307I, determined by CD spectra, was increased by 5.2 degrees C over that of the wild-type enzyme (54.6 degrees C). Activities of both the wild-type and E99K-T307I enzymes, as well as their overall thermostabilities, increased in 1 mM CaCl2. The E99K-T307I enzyme was stable at 55 degrees C with 1 mM CaCl2, reaching 260% of the activity the wild-type enzyme held at 40 degrees C without CaCl2.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s10529-010-0237-5 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!