Cloning and Characterization of Ginsenoside-Hydrolyzing β-Glucosidase from Lactobacillus brevis That Transforms Ginsenosides Rb1 and F2 into Ginsenoside Rd and Compound K

Zhong, Fei-Liang; Ma, Rui; Jiang, Mingliang; Dong, Weiwei; Jiang, Jun; Wu, Songquan; Li, Donghao; Quan, Lin-Hu

doi:10.4014/jmb.1605.05052

Cited by 41 publications

(18 citation statements)

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“…For 1 mg mL −1 initial ginsenoside Rb1 concentration, the conversion rate of 69% was obtained by 10-hour incubation time. 51 In the present study, 95% of the initial ginsenoside Rb1 was converted to ginsenoside Rd by free enzymes only in 15 min incubation time and, for the same incubation duration, the conversion yields of 52.94% and 33.61% were obtained in continuous-flow microreactor experiments for 0.05 and 0.1 mg mL −1 initial ginsenoside Rb1 concentrations, respectively. Immobilization was indicated to cause additional diffusion limitations and low reaction yields in various studies, particularly when focusing on the comparison between free and immobilized enzymes.…”

Section: Batch Enzymatic Hydrolysis Of Ginsenoside Rb1supporting

confidence: 50%

An enzyme immobilized microreactor for continuous‐flow biocatalysis of ginsenoside Rb1

Kazan

Stahl

et al. 2021

J of Chemical Tech & Biotech

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BACKGROUND: Ginsenoside Rb1 is one of the major bioactive components of Panax ginseng C.A. Meyer (Araliaceae), a medicinal plant that has been used for therapeutic purposes for thousands of years in Asian countries. The pharmaceutical activity of ginsenoside Rb1 highly depends on molecular structure and its deglycosylated metabolites are known to be more potent bioactive compounds. However, these deglycosylated ginsenosides do not exist naturally so they are usually obtained by poorly selective methods, like chemical hydrolysis.RESULTS: In this study, the development and characterization of an alginate-based immobilized enzyme microreactor for the catalytic conversion of ginsenoside Rb1 to more bioactive metabolites have been reported. Enzyme kinetic parameters were calculated and characterization tests (such as determination of surface area of alginate matrix, long-term use, and effect of residence time on conversion yield) were conducted. The system was operated under continuous-flow conditions and compared with acidic and batch enzymatic hydrolysis experiments, as conventional approaches. The enzymatic microreactor showed an enhanced activity by producing 13-fold higher amount of ginsenoside F2 than batch enzymatic hydrolysis. CONCLUSION: Obtained results indicated that the newly developed enzymatic microreactor could successfully convert ginsenoside Rb1 to more active metabolites and have a potential for the biocatalysis of multiple ginsenosides, as well as pharmaceutically active compounds.

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Section: Batch Enzymatic Hydrolysis Of Ginsenoside Rb1supporting

confidence: 50%

An enzyme immobilized microreactor for continuous‐flow biocatalysis of ginsenoside Rb1

Kazan

Stahl

et al. 2021

J of Chemical Tech & Biotech

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“…Michlmayr et al (2010) isolated a novel β‐glucosidase from L. brevis SK3 with a molecular weight of 80 kDa. Meanwhile, Zhong et al (2016) obtained a β‐glucosidase (Bgy2) from L. brevis LH8, which is the largest β‐glucosidase found in L. brevis to date with a molecular weight of 123 kDa.…”

Section: Resultsmentioning

confidence: 99%

Cloning and expression of Lactobacillus brevis β‐glucosidase and its effect on the aroma of strawberry wine

Xia

Wang

et al. 2022

Food Processing Preservation

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Aroma is one of the key characteristics of fruit wine and is correlated to volatile organic compounds, which greatly influences the purchase intention of consumers (Zhang, Wang, et al., 2021). Although the major aroma compounds, mainly derived from the fruit, are produced during the alcoholic fermentation stage, a number of odorless non-volatile glycosides are also present, which are often considered as aroma precursors; the hydrolysis of these glycosides could significantly improve the natural aroma compounds of fruit wine (Aaby et al., 2018;Michlmayr et al., 2010). Therefore, researchers have attempted to develop effective methods to hydrolyze these nonvolatile glycosides to release the free aroma compounds (Michlmayr et al., 2010). Lactic acid bacteria (LAB) can hydrolyze glycosylated

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“…Although the utilization of the disaccharides by L. plantarum and L. pentosus in FCJM at pH 3.7 ± 0.1 could occur during a prolonged incubation, β‐glucosidases are inhibited at pH below 4.0 (Kim, Lee, & Ma, 2017; Takase & Horikoshi, 1988; Yeoman et al, 2010; Zhong et al., 2016). While β‐glucosidases occur in many organisms, the activity of the enzymes derived from thermophilic bacteria and lactobacilli is known to be severely compromised at a pH of 4.0 with a 20% enzyme stability, as compared to a 40% stability at pH 5.0 (Kim et al., 2017; Takase & Horikoshi, 1988; Yeoman et al, 2010; Zhong et al., 2016). Growth of L. plantarum is known to stop at a pH of 3.3 with the cessation of acid production at a pH of 3.0 (McDonald, Fleming, & Hassan, 1990).…”

Section: Resultsmentioning

confidence: 99%

Gentiobiose and cellobiose content in fresh and fermenting cucumbers and utilization of such disaccharides by lactic acid bacteria in fermented cucumber juice medium

Ucar

Pérez‐Díaz

Dean

2020

Food Science & Nutrition

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The content of cellobiose and gentiobiose, cellulose-derived dissacharides, in fresh and fermented cucumber was evaluated along with the ability of Lactobacillus plantarum, Lactobacillus pentosus, Lactobacillus buchneri and Lactobacillus brevis to utilize them during and after fermentation. The disaccharide content in fresh and fermenting cucumbers was below the detection level (10 µM) using HPLC for analysis. Utilization of cellobiose and gentiobiose by lactic acid bacteria (LAB) was tested in fermented cucumber juice medium (FCJM), a model system for the bioconversion and postfermentation lacking glucose and fructose. Changes in the fermentation metabolites were followed using HPLC and pH measurements as a function of time. The disaccharides were utilized by L. plantarum, L. pentosus, and L. buchneri in FCJM at pH 4.7 ± 0.1, representative of the active fermentation period, and converted to lactic acid. The disaccharides were not utilized in FCJM at pH 3.7 ± 0.1, representative of the end of fermentation. While L. brevis was unable to utilize cellobiose efficiently in FCJM, they were able to remove gentiobiose at pH 4.7 ± 0.1. Some strain level differences in cellobiose utilization were observed. It is concluded that the disaccharides are absent in the fresh cucumber and the typical fermentation. The LAB prevalent in the bioconversion utilizes cellobiose and gentiobiose, if available, at pH 4.7 ± 0.1. The LAB would not remove the disaccharides, which could become available from cellulose degradation by the acid resistant indigenous microbiota, after the pH is reduced to 3.7 ± 0.1.

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Cloning and Characterization of Ginsenoside-Hydrolyzing β-Glucosidase from Lactobacillus brevis That Transforms Ginsenosides Rb1 and F2 into Ginsenoside Rd and Compound K

Cited by 41 publications

References 0 publications

An enzyme immobilized microreactor for continuous‐flow biocatalysis of ginsenoside Rb1

An enzyme immobilized microreactor for continuous‐flow biocatalysis of ginsenoside Rb1

Cloning and expression of Lactobacillus brevis β‐glucosidase and its effect on the aroma of strawberry wine

Gentiobiose and cellobiose content in fresh and fermenting cucumbers and utilization of such disaccharides by lactic acid bacteria in fermented cucumber juice medium

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