Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus)
The thermal stability and parameters of the Michaelis-Menten kinetics of engineered variant of recombinant reindeer chymosin (Rangifer tarandus) with a point amino acid substitution Lys53→Glu were studied. The values of the threshold of thermal inactivation of the studied enzyme and commercial recom...
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Kemerovo State University
2024
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Online Access: | https://doi.org/10.31515/2073-4018-2023-3-42-44 |
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ftinfram:oai:naukaru.ru:art_73761 2024-02-11T10:08:10+01:00 Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) Pushkarev Vladimir Musina Olga Belenkaya Svetlana Shcherbakov Dmitry Koval Anatoliy Belov Aleksandr Elchaninov Vadim 2024-01-23 https://doi.org/10.31515/2073-4018-2023-3-42-44 ru rus Kemerovo State University 10.31515/2073-4018-2023-3-42-44 https://doi.org/10.31515/2073-4018-2023-3-42-44 Text 2024 ftinfram https://doi.org/10.31515/2073-4018-2023-3-42-44 2024-01-23T17:41:05Z The thermal stability and parameters of the Michaelis-Menten kinetics of engineered variant of recombinant reindeer chymosin (Rangifer tarandus) with a point amino acid substitution Lys53→Glu were studied. The values of the threshold of thermal inactivation of the studied enzyme and commercial recombinant cow chymosin coincided and amounted to 50 °C. The engineered reindeer enzyme showed the greatest affinity to the used chromogenic substrate, its Michaelis constant (Km) was 1,5–4,7 times lower than the same indicator of commercial recombinant chymosins. The catalytic rate constants (kcat) of the engineered variant of deer chymosin and recombinant camel chymosin were comparable. In terms of specificity (kcat/Km), the chymosins of reindeer and cow surpassed the genetically engineered analogue of the chymosin of the single-humped camel by 1,7 times. Text Rangifer tarandus Scientific Publishing Center INFRA - M Cheesemaking and buttermaking 3 42 44 |
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Scientific Publishing Center INFRA - M |
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ftinfram |
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Russian |
description |
The thermal stability and parameters of the Michaelis-Menten kinetics of engineered variant of recombinant reindeer chymosin (Rangifer tarandus) with a point amino acid substitution Lys53→Glu were studied. The values of the threshold of thermal inactivation of the studied enzyme and commercial recombinant cow chymosin coincided and amounted to 50 °C. The engineered reindeer enzyme showed the greatest affinity to the used chromogenic substrate, its Michaelis constant (Km) was 1,5–4,7 times lower than the same indicator of commercial recombinant chymosins. The catalytic rate constants (kcat) of the engineered variant of deer chymosin and recombinant camel chymosin were comparable. In terms of specificity (kcat/Km), the chymosins of reindeer and cow surpassed the genetically engineered analogue of the chymosin of the single-humped camel by 1,7 times. |
format |
Text |
author |
Pushkarev Vladimir Musina Olga Belenkaya Svetlana Shcherbakov Dmitry Koval Anatoliy Belov Aleksandr Elchaninov Vadim |
spellingShingle |
Pushkarev Vladimir Musina Olga Belenkaya Svetlana Shcherbakov Dmitry Koval Anatoliy Belov Aleksandr Elchaninov Vadim Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) |
author_facet |
Pushkarev Vladimir Musina Olga Belenkaya Svetlana Shcherbakov Dmitry Koval Anatoliy Belov Aleksandr Elchaninov Vadim |
author_sort |
Pushkarev Vladimir |
title |
Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) |
title_short |
Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) |
title_full |
Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) |
title_fullStr |
Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) |
title_full_unstemmed |
Thermal stability and Michaelis-Menten kinetics parametersof engineered variant of recombinant reindeer chymosin (Rangifer tarandus) |
title_sort |
thermal stability and michaelis-menten kinetics parametersof engineered variant of recombinant reindeer chymosin (rangifer tarandus) |
publisher |
Kemerovo State University |
publishDate |
2024 |
url |
https://doi.org/10.31515/2073-4018-2023-3-42-44 |
genre |
Rangifer tarandus |
genre_facet |
Rangifer tarandus |
op_relation |
10.31515/2073-4018-2023-3-42-44 https://doi.org/10.31515/2073-4018-2023-3-42-44 |
op_doi |
https://doi.org/10.31515/2073-4018-2023-3-42-44 |
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Cheesemaking and buttermaking |
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3 |
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42 |
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44 |
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