Glycosyl hydrolase catalyzed glycosylation in unconventional media

Chen, Hanchi; Jin, Xiao; Zhu, Linjiang; Lu, Yuele; Ma, Zhi; Liu, Shijie; Chen, Xiaolong

doi:10.1007/s00253-020-10924-1

Cited by 9 publications

(4 citation statements)

References 124 publications

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“…In summary, AGL from O. sativa was expressed in P. pastoris , which proved to be beneficial in fermentation process, allowing the production of enough enzyme and promoting enzymatic synthesis of AA-2G by AGLs. To date, the full potential of rAGL has not been fully realized in this study and further work is needed to improve enzyme activity for transglycosylation, such as controlling the conditions of glycosylation reactions [60] and enzyme technology to create a glycosynthase [61] . These studies will provide the basis for the application of rAGL in AA-2G industrial production.…”

Section: Figure 6 4 Discussionmentioning

confidence: 99%

Extracellular expression and characterization of an α-glucosidase from Oryza sativa and its transglycosylation for synthesis of 2-O-α-D-glucopyranosyl-L-ascorbic acid

Shao

Cheng

et al. 2021

Preprint

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2-O-α-D-Glucopyranosyl-L-ascorbic acid (AA-2G) is an important industrial derivative of L-ascorbic acid (AA), which has the distinct advantages of non-reducibility, antioxidation, and reproducible decomposition into L-ascorbic acid and glucose. Enzymatic synthesis is a preferred method for AA-2G production over alternative chemical synthesis owing to the regioselective glycosylation reaction. α-Glucosidase, an enzyme classed into O- glycoside hydrolases, may be used in glycosylation reactions to synthesize AA-2G. Here, one α-glucosidase from Oryza sativa (rAGL) was recombinantly produced in Pichia pastoris GS115 and used for biosynthesis of AA-2G with few intermediates and byproducts. The extracellular rAGL reached 9.11 U/mL after fed-batch cultivation for 102 h in a 5-L fermenter. The specific activity of purified rAGL is 49.83 U/mg at 37 °C and pH 4.0. The optimal temperature of rAGL was 65 °C, and it was stable below 55 °C. rAGL was active over the range of pH 3.0–7.0, with the maximal activity at pH 4.0. Under the condition of 37 °C , pH 4.0, equimolar maltose and AA·Na, 8.7±0.4 g/L of AA-2G was synthesized by rAGL. These studies lay the basis for the industrial application of recombinant α-glucosidase. Keywords: α-Glucosidase; Oryza sativa; 2-O-α-D-glucopyranosyl-L-ascorbic acid; Transglycosylation; Pichia pastoris

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Section: Figure 6 4 Discussionmentioning

confidence: 99%

Extracellular expression and characterization of an α-glucosidase from Oryza sativa and its transglycosylation for synthesis of 2-O-α-D-glucopyranosyl-L-ascorbic acid

Shao

Cheng

et al. 2021

Preprint

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“…37,38 In that sense, the glycosylation of glycerol could improve certain functional properties that make it valuable, especially, its solubility, stability, and sweetness; as well as its bioavailability. 4,39 In addition, glycerol is generated on a large scale (about 900 000 metric tonnes per year) as a common by-product from soap manufacturing, petroleum rening, and molasses fermentation. 31,33,34,36,40 Consequently, nding novel and clean processes to convert this compound into new molecules with a higher added value may allow the optimization of its integral use and the achievement of greater protability to guarantee the sustainability of the industry and the environment.…”

Section: Solvents Used As Fructosyl-acceptor By Ffasementioning

confidence: 99%

Enzymatic synthesis of novel fructosylated compounds by Ffase from Schwanniomyces occidentalis in green solvents

et al. 2021

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“…The second step (orange box) involves a water molecule attacking the carbohydrate-enzyme linkage, transferring the proton to the active site acid/base carboxylate and releasing glucose. In addition to breaking the glycosidic bonds in sugars, BGLs can also lead to the formation of glycosidic bonds (i.e., transglycosylation) in non-aqueous media with hydroxyl groups [8]. The reaction mechanism is similar to the BGL hydrolysis process, with a slight difference in the second step (Figure 2B, red box) which involves the attack of another sugar molecule (receptor A) rather than a water molecule, leading to transglycosylation [9].…”

Section: Introductionmentioning

confidence: 97%

Recent Advances in β-glucosidase Engineering: A Brief Review

Zhao¹,

Huang²,

Ouyang³

et al. 2023

Preprint

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β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stability, etc. Many approaches have been developed to engineer BGLs to improve these enzymatic characteristics to facilitate industrial production. In this article, we review the recent advances in BGL engineering in the field, including the efforts from our laboratory. We summarize and discuss the BGL engineering studies according to the targeted functions as well as the specific strategies used for BGL engineering.

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Glycosyl hydrolase catalyzed glycosylation in unconventional media

Cited by 9 publications

References 124 publications

Extracellular expression and characterization of an α-glucosidase from Oryza sativa and its transglycosylation for synthesis of 2-O-α-D-glucopyranosyl-L-ascorbic acid

Extracellular expression and characterization of an α-glucosidase from Oryza sativa and its transglycosylation for synthesis of 2-O-α-D-glucopyranosyl-L-ascorbic acid

Enzymatic synthesis of novel fructosylated compounds by Ffase from Schwanniomyces occidentalis in green solvents

Recent Advances in β-glucosidase Engineering: A Brief Review

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