Thermal Stability Enhancement of L-Asparaginase from Corynebacterium glutamicum Based on a Semi-Rational Design and Its Effect on Acrylamide Mitigation Capacity in Biscuits
Huibing Chi, Qingwei Jiang, Yiqian Feng, Guizheng Zhang, Yilian Wang, Ping Zhu, Zhaoxin Lu, Fengxia Lu · 2023
Read Thermal Stability Enhancement of L-Asparaginase from Corynebacterium glutamicum Based on a Semi-Rational Design and Its Effect on Acrylamide Mitigation Capacity in Biscuits by Huibing Chi, Qingwei Jiang, Yiqian Feng, Guizheng Zhang, Yilian Wang, Ping Zhu, Zhaoxin Lu, Fengxia Lu (2023) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-10706719.txt.
Description
Huibing Chi and co-authors hardened this 2023 enzyme that can strip a toxin precursor out of baked food. Acrylamide forms when food browns and carries cancer risk. The enzyme asparaginase breaks down its precursor, but natural versions wilt under heat and work sluggishly. The team redesigned a bacterial version by consensus-guided tweaks and saturation testing at chosen spots.
Their double mutant kept its cutting power while lasting far longer at forty degrees: a half-life of about thirteen minutes against the original's three. Structural models credit a friendlier surface charge pattern. In biscuit trials the mutant cut acrylamide formation as hoped. A heat-tough enzyme could let food makers treat dough before baking without losing the tool to the oven's warmth.
Catalog record
| CREATOR | Huibing Chi, Qingwei Jiang, Yiqian Feng, Guizheng Zhang, Yilian Wang, Ping Zhu, Zhaoxin Lu, Fengxia Lu |
|---|---|
| YEAR | 2023 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 41 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |