Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum
Creatine is a naturally occurring derivative of an amino acid commonly utilized in functional foods and pharmaceuticals. Nevertheless, the current industrial synthesis of creatine relies on chemical processes, which may hinder its utilization in certain applications. Therefore, a biological approach...
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KeAi Communications Co., Ltd.
2024-03-01
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| Series: | Synthetic and Systems Biotechnology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405805X24000036 |
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| author | Chunjian Li Pengdong Sun Guoqing Wei Yuqi Zhu Jingyuan Li Yanfeng Liu Jian Chen Yang Deng |
| author_facet | Chunjian Li Pengdong Sun Guoqing Wei Yuqi Zhu Jingyuan Li Yanfeng Liu Jian Chen Yang Deng |
| author_sort | Chunjian Li |
| collection | DOAJ |
| description | Creatine is a naturally occurring derivative of an amino acid commonly utilized in functional foods and pharmaceuticals. Nevertheless, the current industrial synthesis of creatine relies on chemical processes, which may hinder its utilization in certain applications. Therefore, a biological approach was devised that employs whole-cell biocatalysis in the bacterium Corynebacterium glutamicum, which is considered safe for use in food production, to produce safe-for-consumption creatine. The objective of this study was to identify a guanidinoacetate N-methyltransferase (GAMT) with superior catalytic activity for creatine production. Through employing whole-cell biocatalysis, a gamt gene from Mus caroli (Mcgamt) was cloned and expressed in C. glutamicum ATCC 13032, resulting in a creatine titer of 3.37 g/L. Additionally, the study employed a promoter screening strategy that utilized nine native strong promoters in C. glutamicum to enhance the expression level of GAMT. The highest titer was achieved using the P1676 promoter, reaching 4.14 g/L. The conditions of whole-cell biocatalysis were further optimized, resulting in a creatine titer of 5.42 g/L. This is the first report of successful secretory creatine expression in C. glutamicum, which provides a safer and eco-friendly approach for the industrial production of creatine. |
| first_indexed | 2024-03-07T14:29:22Z |
| format | Article |
| id | doaj.art-b5e7f34660534b3f82caba838df79a36 |
| institution | Directory Open Access Journal |
| issn | 2405-805X |
| language | English |
| last_indexed | 2024-03-07T14:29:22Z |
| publishDate | 2024-03-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Synthetic and Systems Biotechnology |
| spelling | doaj.art-b5e7f34660534b3f82caba838df79a362024-03-06T05:27:58ZengKeAi Communications Co., Ltd.Synthetic and Systems Biotechnology2405-805X2024-03-019199107Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicumChunjian Li0Pengdong Sun1Guoqing Wei2Yuqi Zhu3Jingyuan Li4Yanfeng Liu5Jian Chen6Yang Deng7College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China; Key Laboratory of Special Food Processing (Co-construction by Ministry and Province), Ministry of Agriculture Rural Affairs, Qingdao Agricultural University, Qingdao 266109, China; Shandong Technology Innovation Center of Special Food, Qingdao 266109, China; Qingdao Special Food Research Institute, Qingdao 266109, China; Qingdao Nuoan Baite Biotechnology Co., Ltd., Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China; Key Laboratory of Special Food Processing (Co-construction by Ministry and Province), Ministry of Agriculture Rural Affairs, Qingdao Agricultural University, Qingdao 266109, China; Shandong Technology Innovation Center of Special Food, Qingdao 266109, China; Qingdao Special Food Research Institute, Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China; Key Laboratory of Special Food Processing (Co-construction by Ministry and Province), Ministry of Agriculture Rural Affairs, Qingdao Agricultural University, Qingdao 266109, China; Shandong Technology Innovation Center of Special Food, Qingdao 266109, China; Qingdao Special Food Research Institute, Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China; Key Laboratory of Special Food Processing (Co-construction by Ministry and Province), Ministry of Agriculture Rural Affairs, Qingdao Agricultural University, Qingdao 266109, China; Shandong Technology Innovation Center of Special Food, Qingdao 266109, China; Qingdao Special Food Research Institute, Qingdao 266109, ChinaCollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China; Key Laboratory of Special Food Processing (Co-construction by Ministry and Province), Ministry of Agriculture Rural Affairs, Qingdao Agricultural University, Qingdao 266109, China; Shandong Technology Innovation Center of Special Food, Qingdao 266109, China; Qingdao Special Food Research Institute, Qingdao 266109, ChinaQingdao Special Food Research Institute, Qingdao 266109, China; Science Center for Future Foods, Engineering Research Center of Ministry of Education on Food Synthetic Biotechnology, and Jiangsu Province Engineering Research Center of Food Synthetic Biotechnology, Jiangnan University, Wuxi 214122, China; Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, ChinaQingdao Special Food Research Institute, Qingdao 266109, China; Science Center for Future Foods, Engineering Research Center of Ministry of Education on Food Synthetic Biotechnology, and Jiangsu Province Engineering Research Center of Food Synthetic Biotechnology, Jiangnan University, Wuxi 214122, China; Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China; Corresponding author. Qingdao Special Food Research Institute, Qingdao 266109, China.College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China; Key Laboratory of Special Food Processing (Co-construction by Ministry and Province), Ministry of Agriculture Rural Affairs, Qingdao Agricultural University, Qingdao 266109, China; Shandong Technology Innovation Center of Special Food, Qingdao 266109, China; Qingdao Special Food Research Institute, Qingdao 266109, China; Corresponding author. College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China.Creatine is a naturally occurring derivative of an amino acid commonly utilized in functional foods and pharmaceuticals. Nevertheless, the current industrial synthesis of creatine relies on chemical processes, which may hinder its utilization in certain applications. Therefore, a biological approach was devised that employs whole-cell biocatalysis in the bacterium Corynebacterium glutamicum, which is considered safe for use in food production, to produce safe-for-consumption creatine. The objective of this study was to identify a guanidinoacetate N-methyltransferase (GAMT) with superior catalytic activity for creatine production. Through employing whole-cell biocatalysis, a gamt gene from Mus caroli (Mcgamt) was cloned and expressed in C. glutamicum ATCC 13032, resulting in a creatine titer of 3.37 g/L. Additionally, the study employed a promoter screening strategy that utilized nine native strong promoters in C. glutamicum to enhance the expression level of GAMT. The highest titer was achieved using the P1676 promoter, reaching 4.14 g/L. The conditions of whole-cell biocatalysis were further optimized, resulting in a creatine titer of 5.42 g/L. This is the first report of successful secretory creatine expression in C. glutamicum, which provides a safer and eco-friendly approach for the industrial production of creatine.http://www.sciencedirect.com/science/article/pii/S2405805X24000036CreatineCorynebacterium glutamicumWhole-cell biocatalysisGuanidinoacetate N-MethyltransferaseFood additive |
| spellingShingle | Chunjian Li Pengdong Sun Guoqing Wei Yuqi Zhu Jingyuan Li Yanfeng Liu Jian Chen Yang Deng Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum Synthetic and Systems Biotechnology Creatine Corynebacterium glutamicum Whole-cell biocatalysis Guanidinoacetate N-Methyltransferase Food additive |
| title | Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum |
| title_full | Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum |
| title_fullStr | Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum |
| title_full_unstemmed | Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum |
| title_short | Efficient biosynthesis of creatine by whole-cell catalysis from guanidinoacetic acid in Corynebacterium glutamicum |
| title_sort | efficient biosynthesis of creatine by whole cell catalysis from guanidinoacetic acid in corynebacterium glutamicum |
| topic | Creatine Corynebacterium glutamicum Whole-cell biocatalysis Guanidinoacetate N-Methyltransferase Food additive |
| url | http://www.sciencedirect.com/science/article/pii/S2405805X24000036 |
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