Biosynthesis of l -theanine via one-step purification and immobilization enzyme system
l-theanine, a non-protein amino acid derived from green tea, was synthesized by a relatively substantial amount of γ-glutamylmethylamide synthetase (GMAS) and polyphosphate kinase (PPK) without efficient recycling. This study establishes a cost-efficient, industrially scalable, and continuous biocat...
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| Published in | Journal of applied microbiology Vol. 136; no. 3 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
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03.03.2025
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| Abstract | l-theanine, a non-protein amino acid derived from green tea, was synthesized by a relatively substantial amount of γ-glutamylmethylamide synthetase (GMAS) and polyphosphate kinase (PPK) without efficient recycling. This study establishes a cost-efficient, industrially scalable, and continuous biocatalytic platform for sustainable l-theanine production.
A functional catalyst system was engineered by fusing GMAS and PPK with the cell wall-binding domain derived from the Listeria monocytogenes p60 protein (Lm-p60). The enzyme complex was immobilized onto Gram-positive enhancer matrix particles, enabling facile separation and reuse over catalytic cycles. The enzymes were reusable and could be applied for six cycles with an l-theanine yield achieving 86%-93%.
The reusable catalyst demonstrates operational sustainability over multiple cycles, offering cost savings and continuous utility. |
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| AbstractList | l-theanine, a non-protein amino acid derived from green tea, was synthesized by a relatively substantial amount of γ-glutamylmethylamide synthetase (GMAS) and polyphosphate kinase (PPK) without efficient recycling. This study establishes a cost-efficient, industrially scalable, and continuous biocatalytic platform for sustainable l-theanine production.
A functional catalyst system was engineered by fusing GMAS and PPK with the cell wall-binding domain derived from the Listeria monocytogenes p60 protein (Lm-p60). The enzyme complex was immobilized onto Gram-positive enhancer matrix particles, enabling facile separation and reuse over catalytic cycles. The enzymes were reusable and could be applied for six cycles with an l-theanine yield achieving 86%-93%.
The reusable catalyst demonstrates operational sustainability over multiple cycles, offering cost savings and continuous utility. l-theanine, a non-protein amino acid derived from green tea, was synthesized by a relatively substantial amount of γ-glutamylmethylamide synthetase (GMAS) and polyphosphate kinase (PPK) without efficient recycling. This study establishes a cost-efficient, industrially scalable, and continuous biocatalytic platform for sustainable l-theanine production.AIMSl-theanine, a non-protein amino acid derived from green tea, was synthesized by a relatively substantial amount of γ-glutamylmethylamide synthetase (GMAS) and polyphosphate kinase (PPK) without efficient recycling. This study establishes a cost-efficient, industrially scalable, and continuous biocatalytic platform for sustainable l-theanine production.A functional catalyst system was engineered by fusing GMAS and PPK with the cell wall-binding domain derived from the Listeria monocytogenes p60 protein (Lm-p60). The enzyme complex was immobilized onto Gram-positive enhancer matrix particles, enabling facile separation and reuse over catalytic cycles. The enzymes were reusable and could be applied for six cycles with an l-theanine yield achieving 86%-93%.METHODS AND RESULTSA functional catalyst system was engineered by fusing GMAS and PPK with the cell wall-binding domain derived from the Listeria monocytogenes p60 protein (Lm-p60). The enzyme complex was immobilized onto Gram-positive enhancer matrix particles, enabling facile separation and reuse over catalytic cycles. The enzymes were reusable and could be applied for six cycles with an l-theanine yield achieving 86%-93%.The reusable catalyst demonstrates operational sustainability over multiple cycles, offering cost savings and continuous utility.CONCLUSIONSThe reusable catalyst demonstrates operational sustainability over multiple cycles, offering cost savings and continuous utility. |
| Author | Fan, Chao Zhang, Chunzhi Qi, Jiakun |
| Author_xml | – sequence: 1 givenname: Chao surname: Fan fullname: Fan, Chao – sequence: 2 givenname: Jiakun surname: Qi fullname: Qi, Jiakun – sequence: 3 givenname: Chunzhi surname: Zhang fullname: Zhang, Chunzhi |
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| Cites_doi | 10.1039/D3GC00027C 10.1016/j.synbio.2022.11.006 10.3390/molecules25041002 10.1016/j.enzmictec.2020.109644 10.1016/j.tifs.2021.06.006 10.1271/bbb.70663 10.1186/s12870-017-1096-1 10.1080/21655979.2015.1040956 10.3390/molecules16076041 10.3892/mmr.2018.9459 10.1038/srep21151 10.1007/s00253-015-6967-5 10.1016/j.enzmictec.2024.110481 10.4014/jmb.1910.10044 10.1007/s10295-020-02305-4 10.1016/j.ijbiomac.2018.11.047 10.1016/j.mtbio.2023.100580 10.1016/j.biotechadv.2022.108016 10.14218/ERHM.2020.00048 10.1016/j.enzmictec.2022.109997 10.1007/s00253-019-10252-z 10.1271/bbb.70462 10.1080/21655979.2016.1200772 10.1111/j.1365-2958.2008.06211.x 10.1080/07388551.2018.1531822 10.1002/cbic.201402550 10.1371/journal.pone.0072167 10.1007/s00253-015-6498-0 10.1038/mi.2009.131 |
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| Keywords | anchoring tags GEM particles one-step purification and immobilization (OSPI) l-theanine production |
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| SubjectTerms | Amide Synthases - genetics Amide Synthases - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Biocatalysis Enzymes, Immobilized - genetics Enzymes, Immobilized - metabolism Escherichia coli - genetics Glutamates - biosynthesis Listeria monocytogenes - enzymology Listeria monocytogenes - genetics Phosphotransferases (Phosphate Group Acceptor) - genetics Phosphotransferases (Phosphate Group Acceptor) - metabolism |
| Title | Biosynthesis of l -theanine via one-step purification and immobilization enzyme system |
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