Enhanced d-tagatose production by spore surface-displayed l-arabinose isomerase from isolated Lactobacillus brevis PC16 and biotransformation

Guo, Qi; An, Yi; Yun, Jimmy; Yang, Miaomiao; Magocha, Tinashe Archbold; Zhu, Jingfei; Xue, Yanbo; Qi, Yilin; Zabed, Hossain M.; Sun, Wenjing; Qi, Xianghui

doi:10.1016/j.biortech.2017.09.187

Cited by 54 publications

(35 citation statements)

References 35 publications

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“…The mobile phase was pure water running at a flowrate of 0.5 mL/min. A sample volume of 10 µL was injected to the column temperature (80ºC) [1].…”

Section: D-tagatose Productionmentioning

confidence: 99%

“…The rare sugar monosaccharide D-tagatose, which has the advantage of having low calorific content, accompanied by more than 90% sweetness compared to sucrose. As D-tagatose has been classified by the US Food and Drug Administration (FDA) to be generally recognized as safe (GRAS), it is considered as a promising sweetener that can be utilized in various applications in food industries [1][2][3]. Due to its relative low glycemic index, it can be considered as an alternative to glucose by playing an important role in mitigating the effect on hyperglycemia, type-2 diabetes, probiotic function, and antioxidant activity [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

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Screening and Identification of Lactic Acid Bacteria with D-tagatose Production Capability

Wen

Zhou

Huang

et al. 2019

BJI

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Aims: D-tagatose is a natural ketohexose which can be used as a functional sweetener in foods, diary and beverages products. Isolation of new bacterial strains having the ability to produce Dtagatose is a continuously trending topic of research. Study Design: Screening of strains with D-tagatose production by identification and determination of its ability to produce D-tagatose content. Place and Duration of Study: School of Food and Biological Engineering, Jiangsu University between May 2018 and April 2019. Methodology: We initially screened and identified the strains capable of producing D-tagatose through kimchi liquid, and determined the species and genetic characteristics of the strain by physiological, biochemical and molecular biological identification, and then determined the content of D-tagatose by high performance liquid chromatography. Finally calculate the ability of the strain to produce D-tagatose. Li et al.; BJI, 23(2): 1-6, 2019; Article no.BJI.49412 2 Results: In this study, 4 strains of lactic acid bacteria (LAB) were isolated from kimchi sample. The isolates were identified as Lactobacillus spp. (Lactobacillus plantarum, Lactobacillus fermentum and Lactobacillus salivarius) on the basis of morphological, physicochemical characteristics and analysis of 16S rDNA gene sequence. Because of the novelty, strain designated as L. salivarius UJS 003 was considered for D-tagatose yield. Fermentation of D-tagatose was carried out using galactose as substrate for 48 hr at 37 °C, and HPLC method was used to determine the yield. The experimental results exhibited a D-tagatose yield of 3.134 g/L by L. salivarius UJS 003. Conclusion: The strain UJS 003 represented as a potent D-tagatose producer and could be useful in a variety of biotechnological and industrial processes, particularly food and beverage industries. Short Research Article

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“…The mobile phase was pure water running at a flowrate of 0.5 mL/min. A sample volume of 10 µL was injected to the column temperature (80ºC) [1].…”

Section: D-tagatose Productionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Screening and Identification of Lactic Acid Bacteria with D-tagatose Production Capability

Wen

Zhou

Huang

et al. 2019

BJI

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“…Thus, the system described here demonstrates how to overcome three major limitations of enzymatic catalysis (stability, thermodynamic, kinetic) for tagatose production using LAI. We believe that a similar strategy may be applicable to other biocatalytic systems as well – particularly lyases 52 , translgycosidases 53 , and isomerases 17,25,54,55 – where free enzyme performance is poor due to stability, thermodynamic, and/or kinetic limitations.…”

Section: Discussionmentioning

confidence: 99%

Surpassing thermodynamic, kinetic, and stability barriers to isomerization catalysis for tagatose biosynthesis

Bober

Nair

2019

Preprint

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3There are many enzymes that are relevant for making rare and valuable chemicals that 4 while active, are severely limited by thermodynamic, kinetic, or stability issues (e.g. 5 isomerases, lyases, transglycosidase etc.). In this work, we study an enzymatic reaction 6 system − Lactobacillus sakei L-arabinose isomerase (LsLAI) for D-galactose to D-tagatose 7 isomerizationthat is limited by all three reaction parameters. The enzyme has a low 8 catalytic efficiency for non-natural substrate galactose, has low thermal stability at 9 temperatures > 40 °C, and equilibrium conversion < 50%. After exploring several strategies 10 to overcome these limitations, we finally show that encapsulating the enzyme in a gram-11 positive bacterium (Lactobacillus plantarum) that is chemically permeabilized can enable 12 reactions at high rates, high conversion, and at high temperatures. The modified whole cell 13 system stabilizes the enzyme, differentially partitions substrate and product across the 14 membrane to shift the equilibrium toward product formation enables rapid transport of 15 substrate and product for fast kinetics. In a batch process, this system enables 16 approximately 50 % conversion in 4 h starting with 300 mM galactose (an average 17 productivity of 37 mM/h), and 85 % conversion in 48 h, which are the highest reported for 18 food-safe mesophilic tagatose synthesis. We suggest that such an approach may be 19 invaluable for other enzymatic processes that are similarly kinetically-, thermodynamically-20 , and/or stability-limited. 65We use the food-safe engineered probiotic bacterium Lactobacillus plantarum as the 66 expression host due to its increasing relevance to biochemical and biomedical research 30,31 . 67This approach enabled ~ 50 % conversion of galactose to tagatose in 4 h (productivity of ~ 68 38 mmol tagatose L -1 h -1 ) ultimately reaching ~ 85% conversion after 48 h at high galactose 69 loading (300 mM) in batch culture. This is among the highest conversions and 70 productivities reported to date for tagatose production using a mesophilic enzyme. Such an 71 approach is expected to be applicable to other biocatalytic systems where similar trade-offs 72 between kinetics, thermodynamics, and/or stability pose hurdles to process development. 73 74 Results: 75Characterizing L. sakei LAI (LsLAI) limitations. 76 At high substrate loading (400mM galactose) and 37 °C, the reported optimal temperature 77 for this enzyme 32 , LsLAI purified from L. plantarum exhibited an initial forward reaction 78 (turnover) rate (kinitial) of 9.3 ± 0.3 s -1 , which is lower than the maximum reaction rate 79 possible by this enzyme of 17.0 ± 1.3 s -1 min -1 with its preferred substrate, arabinose, at 400 80 mM. Increasing the reaction temperature to 50 °C increased the initial reaction rate to 11.2 81 s -1 ( Fig. 1a) but was accompanied by rapid enzyme inactivation, which is consistent with 82 previous reports of thermal instability of this enzyme 32 . The enzyme exhibited first-order 83 degradation with a half-life (t½) ...

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“…However, the increase of pH and accumulation of product cadaverine during the reaction process could cause inactivation of CadA . Further, non-recyclable of free enzyme increases the cost, which inhibits its practical application (Singh and Kayastha, 2012;Guo et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Cadaverine Production From L-Lysine With Chitin-Binding Protein-Mediated Lysine Decarboxylase Immobilization

Zhou

Zhang

Wei

et al. 2020

Front. Bioeng. Biotechnol.

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Lysine decarboxylase (CadA) can directly convert L-lysine to cadaverine, which is an important platform chemical that can be used to produce polyamides. However, the non-recyclable and the poor pH tolerance of pure CadA hampered its practical application. Herein, a one-step purification and immobilization procedure of CadA was established to investigate the cadaverine production from L-lysine. Renewable biomass chitin was used as a carrier for lysine decarboxylase (CadA) immobilization via fusion of a chitin-binding domain (ChBD). Scanning electron microscopy, laser scanning confocal microscopy, fourier transform infrared spectra, elemental analysis, and thermal gravimetric analysis proved that the fusion protein ChBD-CadA can be adsorbed on chitin effectively. Furthermore, the fusion protein (ChBD-CadA) existed better pH stability compared to wild CadA, and kept over 73% of the highest activity at pH 8.0. Meanwhile, the ChBD-CadA showed high specificity toward chitin and reached 93% immobilization yield within 10 min under the optimum conditions. The immobilized ChBD-CadA (I-ChBD-CadA) could efficiently converted L-lysine at 200.0 g/L to cadaverine at 135.6 g/L in a batch conversion within 120 min, achieving a 97% molar yield of the substrate L-lysine. In addition, the I-ChBD-CadA was able to be reused under a high concentration of L-lysine and retained over 57% of its original activity after four cycles of use without acid addition to maintain pH. These results demonstrate that immobilization of CadA using chitin-binding domain has the potential in cadaverine production on an industrial scale.

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Enhanced d-tagatose production by spore surface-displayed l-arabinose isomerase from isolated Lactobacillus brevis PC16 and biotransformation

Cited by 54 publications

References 35 publications

Screening and Identification of Lactic Acid Bacteria with D-tagatose Production Capability

Screening and Identification of Lactic Acid Bacteria with D-tagatose Production Capability

Surpassing thermodynamic, kinetic, and stability barriers to isomerization catalysis for tagatose biosynthesis

Cadaverine Production From L-Lysine With Chitin-Binding Protein-Mediated Lysine Decarboxylase Immobilization

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