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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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Bibliographic Details
Published in:Applied biochemistry and microbiology 2021-12, Vol.57 (9), p.917-924
Main Authors: Gorbunov, A. A., Akentyev, F. I., Gubaidullin, I. I., Zhiganov, N. I., Tereshchenkova, V. F., Elpidina, E. N., Kozlov, D. G.
Format: Article
Language:English
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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.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683821090039