AI Article Synopsis
- The manuscript discusses the cloning and expression of Tk2246, a plant-type L-asparaginase, and improvements made to increase its soluble production.
- Various strategies significantly enhanced the yield of soluble Tk2246, which was found to be produced even without an inducer, sometimes in a partially cleaved form.
- When tested for acrylamide mitigation, Tk2246 demonstrated over 80% reduction in acrylamide levels in different foods and also showed antistaling properties, making it a promising candidate for use in the food industry.
Article Abstract
This manuscript describes enhancement of soluble production, auto-cleavage analysis and assessment of acrylamide mitigation potential of Tk2246, a plant-type L-asparaginase from . The gene encoding Tk2246 was cloned and expressed in . Recombinant Tk2246 was produced mainly in insoluble form. Various strategies were utilized to enhance the soluble production, which significantly increased the soluble yield. Interestingly, recombinant Tk2246 was produced even without addition of the inducer, though relatively in a lower amount. To our surprise, Tk2246 was produced in partially cleaved form when the inducer was not added in the culture. When applied for acrylamide mitigation, Tk2246 reduced the acrylamide formation more than 80% in French fries, chapati and yeast-leavened bread. In addition to acrylamide mitigation, Tk2246 exhibited antistaling activity without loss of sensory properties of the food. High activity, thermostability and efficient acrylamide reduction capability make Tk2246 a potential candidate for industrial applications.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9123126 | PMC |
| http://dx.doi.org/10.1007/s13205-022-03197-0 | DOI Listing |
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