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Biosynthesis and Secretion of Serine Peptidase SerP38 from Tenebrio molitor in the Yeast Komagataella kurtzmanii
A strain of the yeast Komagataella kurtzmanii , a producer of recombinant peptidase SerP38 from the yellow mealworm Tenebrio molitor , has been obtained. The level of proenzyme secretion was 20–50 mg/L. It was shown that the target His 6 -tagged protein was produced in two forms during secretion in...
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Published in: | Applied biochemistry and microbiology 2021-12, Vol.57 (9), p.917-924 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | A strain of the yeast
Komagataella kurtzmanii
, a producer of recombinant peptidase SerP38 from the yellow mealworm
Tenebrio molitor
, has been obtained. The level of proenzyme secretion was 20–50 mg/L. It was shown that the target His
6
-tagged protein was produced in two forms during secretion in yeast. One of them was a monomer that was efficiently purified via Ni-NTA chromatography and then activated with trypsin. Another form accumulated in the culture medium as oligomers prone to aggregation in the presence of Ni
2+
ions and was not activated by trypsin treatment. Aggregation is likely the result of the polypeptide-chain misfolding. |
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ISSN: | 0003-6838 1608-3024 |
DOI: | 10.1134/S0003683821090039 |