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Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp.: cloning, expression and characterization
The N-terminal amino acid sequence of the Pleurotus sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from P. ostreatus PC 15 v2.0. The length of the Pleurotus sp. trehalase gene was 2247 bp, encoding a protein of 7...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Mycological Society of Japan
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10024966/ https://www.ncbi.nlm.nih.gov/pubmed/37089524 http://dx.doi.org/10.47371/mycosci.2022.09.001 |
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author | Tsutsumi, Gaku Kuroki, Chikako Kamei, Kengo Kusuda, Mizuho Nakazawa, Masami Sakamoto, Tatsuji Ishikawa, Mariko Harada, Shinji Kobayashi, Hitoshi Ouchi, Kenji Inatomi, Satoshi Sakaguchi, Minoru Iwamoto, Takeo Ueda, Mitsuhiro |
author_facet | Tsutsumi, Gaku Kuroki, Chikako Kamei, Kengo Kusuda, Mizuho Nakazawa, Masami Sakamoto, Tatsuji Ishikawa, Mariko Harada, Shinji Kobayashi, Hitoshi Ouchi, Kenji Inatomi, Satoshi Sakaguchi, Minoru Iwamoto, Takeo Ueda, Mitsuhiro |
author_sort | Tsutsumi, Gaku |
collection | PubMed |
description | The N-terminal amino acid sequence of the Pleurotus sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from P. ostreatus PC 15 v2.0. The length of the Pleurotus sp. trehalase gene was 2247 bp, encoding a protein of 749 amino acids with a predicted molecular mass of 81.2 kDa. The molecular mass of the recombinant enzyme was estimated to be about 117 kDa by SDS-PAGE. We found that the recombinant enzyme comprised an N-glycosylated sugar chain and that its optimum pH and temperature were 4.5 and 40 ºC, respectively. Moreover, this enzyme exhibited high activity against trehalose exclusively. We found that the enzyme is novel acid trehalase belonging to GH family 37. |
format | Online Article Text |
id | pubmed-10024966 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Mycological Society of Japan |
record_format | MEDLINE/PubMed |
spelling | pubmed-100249662023-04-20 Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp.: cloning, expression and characterization Tsutsumi, Gaku Kuroki, Chikako Kamei, Kengo Kusuda, Mizuho Nakazawa, Masami Sakamoto, Tatsuji Ishikawa, Mariko Harada, Shinji Kobayashi, Hitoshi Ouchi, Kenji Inatomi, Satoshi Sakaguchi, Minoru Iwamoto, Takeo Ueda, Mitsuhiro Mycoscience Full Paper The N-terminal amino acid sequence of the Pleurotus sp. 90 kDa protein was in good agreement with the corresponding sequence of the glycoside hydrolase (GH) family 37 protein (trehalase) from P. ostreatus PC 15 v2.0. The length of the Pleurotus sp. trehalase gene was 2247 bp, encoding a protein of 749 amino acids with a predicted molecular mass of 81.2 kDa. The molecular mass of the recombinant enzyme was estimated to be about 117 kDa by SDS-PAGE. We found that the recombinant enzyme comprised an N-glycosylated sugar chain and that its optimum pH and temperature were 4.5 and 40 ºC, respectively. Moreover, this enzyme exhibited high activity against trehalose exclusively. We found that the enzyme is novel acid trehalase belonging to GH family 37. The Mycological Society of Japan 2022-10-21 /pmc/articles/PMC10024966/ /pubmed/37089524 http://dx.doi.org/10.47371/mycosci.2022.09.001 Text en 2022, by The Mycological Society of Japan https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open-access paper distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivative 4.0 international license (CC BY-NC-ND 4.0: https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Full Paper Tsutsumi, Gaku Kuroki, Chikako Kamei, Kengo Kusuda, Mizuho Nakazawa, Masami Sakamoto, Tatsuji Ishikawa, Mariko Harada, Shinji Kobayashi, Hitoshi Ouchi, Kenji Inatomi, Satoshi Sakaguchi, Minoru Iwamoto, Takeo Ueda, Mitsuhiro Novel acid trehalase belonging to glycoside hydrolase family 37 from Pleurotus sp.: cloning, expression and characterization |
title | Novel acid trehalase belonging to
glycoside hydrolase family 37 from Pleurotus sp.:
cloning, expression and characterization |
title_full | Novel acid trehalase belonging to
glycoside hydrolase family 37 from Pleurotus sp.:
cloning, expression and characterization |
title_fullStr | Novel acid trehalase belonging to
glycoside hydrolase family 37 from Pleurotus sp.:
cloning, expression and characterization |
title_full_unstemmed | Novel acid trehalase belonging to
glycoside hydrolase family 37 from Pleurotus sp.:
cloning, expression and characterization |
title_short | Novel acid trehalase belonging to
glycoside hydrolase family 37 from Pleurotus sp.:
cloning, expression and characterization |
title_sort | novel acid trehalase belonging to
glycoside hydrolase family 37 from pleurotus sp.:
cloning, expression and characterization |
topic | Full Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10024966/ https://www.ncbi.nlm.nih.gov/pubmed/37089524 http://dx.doi.org/10.47371/mycosci.2022.09.001 |
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