AI Article Synopsis
- Thermostable α-amylases, particularly the one derived from BLA, show high thermal and pH stability, making them valuable for industrial use.
- The recombinant α-amylase Pic-BLA, produced without antibiotic resistance genes in yeast, achieved an impressive amylase activity of 900 U/mL and exhibited a significant increase in molecular mass due to deep glycosylation.
- Comparisons of thermostability between glycosylated Pic-BLA and non-glycosylated Eco-BLA indicate that glycosylation has minimal impact on the enzyme's heat tolerance.
Article Abstract
Thermostable α-amylases are widely used in industry. The α-amylase from (BLA) with six potential glycosylation sites possessed excellent thermal and pH stability and high activity. Here, it was expressed in . The Pic-BLA-producing yeast without any antibiotics-resistant gene was cultivated in flasks and the amylase activity in fermentation supernatant reached 900 U/mL. The recombinant α-amylase Pic-BLA produced in was deeply glycosylated with 30% increase in molecular mass (MM). The deglycosylation treatment by Endoglycosidase H (Endo H) reduced the MM of Pic-BLA. Thermostability analysis showed that Pic-BLA and deglycosylated Pic-BLA were similar in heat tolerance. In order to eliminate the extra impact of Endo H, the BLA was also expressed in to get non-glycosylated Eco-BLA. A comparative study between non-glycosylated Eco-BLA and glycosylated Pic-BLA showed no obvious difference in thermostability. It is speculated that the glycosylation has little effect on the thermostability of α-amylase BLA.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6820627 | PMC |
| http://dx.doi.org/10.1007/s13205-019-1943-x | DOI Listing |
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