An efficient method for the high-yield production of l-theanine using a newly isolated glutaminase-producing organism

Shuai, Yuying; Zhang, Tao; Jiang, Bo; Hua, Ying; Mu, Chaofeng

doi:10.1016/j.fbio.2019.02.001

Cited by 21 publications

(14 citation statements)

References 22 publications

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“…The latest study provided a highly efficient method for the Ltheanine producing by permeabilizing P. nitroreducens. 38 The Lglutaminase from permeabilized P. nitroreducens SP.001 cells produced 0.49 M L-theanine with a 66.1% conversion rate and a 45.1 mM/h•L production intensity. 38 In addition, fungus Lglutaminases produced by Trichoderma koningii were also identified and valued to synthesize L-theanine.…”

Section: Methods For L-theanine Productionmentioning

confidence: 99%

“…38 The Lglutaminase from permeabilized P. nitroreducens SP.001 cells produced 0.49 M L-theanine with a 66.1% conversion rate and a 45.1 mM/h•L production intensity. 38 In addition, fungus Lglutaminases produced by Trichoderma koningii were also identified and valued to synthesize L-theanine. 39 The response surface methodology analysis indicated the enzyme solution volume had the most increasing effect on L-theanine concentration.…”

Section: Methods For L-theanine Productionmentioning

confidence: 99%

“…The latest study provided a highly efficient method for the l -theanine producing by permeabilizing P. nitroreducens . The l -glutaminase from permeabilized P.…”

Section: Methods For L-theanine Productionmentioning

confidence: 99%

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From Tea Leaves to Factories: A Review of Research Progress in l-Theanine Biosynthesis and Production

Chen

Wang

Yuan

et al. 2021

J. Agric. Food Chem.

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l-Theanine is the most popular nonprotein amino acid contained in tea leaves. It is one of the umami components of green tea, contributing to the unique flavor of tea. Because of its various health functions, l-theanine has been commercially developed as a valuable ingredient easily used for various applications in food and pharmaceutical industries. Nowadays, l-theanine is mass-produced by plant extraction, chemical synthesis, or enzymatic transformation in factories. This review embodies the available up to date information on the l-theanine synthesis metabolism in the tea plant as well as approaches to produce it, placing emphasis on the biotransformation of l-theanine. It also gives insight into the challenges of l-theanine production on a large scale, as well as directions for future research. This review comprehensively summarizes information on l-theanine to provide an approach for an in-depth study of l-theanine production.

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Section: Methods For L-theanine Productionmentioning

confidence: 99%

Section: Methods For L-theanine Productionmentioning

confidence: 99%

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From Tea Leaves to Factories: A Review of Research Progress in l-Theanine Biosynthesis and Production

Chen

Wang

Yuan

et al. 2021

J. Agric. Food Chem.

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“…The microorganism used in the present study was P. nitroreducens SP.001 obtained using the method described in our previous study . 17 Pseudomonas nitroreducens SP.001 was cultured in the medium containing 15 g L −1 glucose, 1 g L −1 yeast extract, 10 g L −1 sodium glutamate, 0.5 g L −1 MgSO 4 ·7H 2 O, 0.5 g L −1 KH 2 PO 4 and 0.08 g L −1 ethylenediaminetetraacetic acid (pH 7.0) at 30 °C in a rotary shaker (200 rpm) for 24 h. Then, the fermentation broth was centrifuged (10 000 × g for 10 min; Avanti J‐26XP centrifuge; Beckman Coulter, Fullerton, CA, USA) at 4 °C to remove insoluble materials.…”

Section: Methodsmentioning

confidence: 99%

“…In the present study, P. nitroreducens SP.001 with high intracellular l ‐glutaminase activity, which was screened in our previous study, 17 was permeabilized to increase its enzyme activity. Then, the permeabilized cells were immobilized in calcium alginate gel, and the optimal conditions for cell immobilization were determined.…”

Section: Introductionmentioning

confidence: 99%

Permeabilization and immobilization of whole‐cell Pseudomonas nitroreducensSP.001 to improve its l‐glutaminase performance

et al. 2020

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BACKGROUND L‐Glutaminase is considered to be an important industrial enzyme in both the pharmaceutical and food industries, especially for producing functional glutamyl compounds, such as l‐theanine. Pseudomonas nitroreducens SP.001 with intracellular l‐glutaminase activity has been screened previously. In the present study, three physical permeabilization methods were used to improve l‐glutaminase activity. Then, the whole‐cell immobilization conditions of permeabilized cells using sodium alginate as an embedding agent were optimized to enhance the enzyme's stability and reusability. The characteristics of the immobilized cells were investigated in comparison with those of permeabilized cells. RESULTS The results obtained showed that cell permeabilization using osmotic shock with 155 g L−1 sucrose markedly improved enzyme activity. Then, an effective procedure for immobilization of permeabilized P. nitroreducens cells was established. The optimum conditions for cell immobilization were: sodium alginate 40 g L−1, calcium chloride 30 g L−1, cell mass 100 g L−1 and a curing time of 3 h. After successful immobilization, characterization studies revealed that the thermostability and pH resistance of l‐glutaminase from immobilized cells were enhanced compared to those from permeabilized cells. Moreover, the immobilized biocatalyst could be reused up to 10 times and retained 80% of its activity. CONCLUSION The stability and reusability of the permeabilized cells were improved through the immobilization. These findings indicated that immobilized whole‐cell l‐glutaminase from P. nitroreducens SP.001 possesses more potential for various industrial biotechnological applications than free cells. © 2020 Society of Chemical Industry

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l‐Theanine Goes Greener: A Highly Efficient Bioprocess Catalyzed by the Immobilized γ‐Glutamyl Transferase from Bacillus subtilis

et al. 2023

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l-Theanine (l-Th) was synthesized by simply mixing the reactants (l-glutamine and ethylamine in water) at 25 °C and Bacillus subtilis γ-glutamyl transferase (BsGGT) covalently immobilized on glyoxyl-agarose according to a methodology previously reported by our research group; neither buffers, nor other additives were needed. Ratio of l-glutamine (donor) to ethylamine (acceptor), pH, enzymatic units (IU), and reaction time were optimized (molar ratio of donor/acceptor = 1 : 8, pH 11.6, 1 IU mL À 1 , 6 h), furnishing l-Th in 93 % isolated yield (485 mg, 32.3 g L À 1 ) and high purity (99 %), after a simple filtration of the immobilized biocatalyst, distillation of the volatiles (unreacted ethylamine) and direct lyophilization. Immobilized BsGGT was re-used (four reaction cycles) with 100 % activity retention. This enzymatic synthesis represents a straightforward, fast, high-yielding, and easily scalable approach to l-Th preparation, besides having a favorable green chemistry metrics.

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An efficient method for the high-yield production of l-theanine using a newly isolated glutaminase-producing organism

Cited by 21 publications

References 22 publications

From Tea Leaves to Factories: A Review of Research Progress in l-Theanine Biosynthesis and Production

From Tea Leaves to Factories: A Review of Research Progress in l-Theanine Biosynthesis and Production

Permeabilization and immobilization of whole‐cell Pseudomonas nitroreducensSP.001 to improve its l‐glutaminase performance

l‐Theanine Goes Greener: A Highly Efficient Bioprocess Catalyzed by the Immobilized γ‐Glutamyl Transferase from Bacillus subtilis

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