Sustainable Production of Dihydroxybenzene Glucosides Using Immobilized Amylosucrase from Deinococcus geothermalis
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초록
The amylosucrase encoding gene from Deinococcus geothermalis DSM 11300 (DgAS) was codonoptimized and expressed in Escherichia coli. The enzyme was employed for biosynthesis of three different dihydroxybenzene glucosides using sucrose as the source of glucose moiety. The reaction parameters, including temperature, pH, and donor (sucrose) and acceptor substrate concentrations, were optimized to increase the production yield. This study demonstrates the highest ever reported molar yield of hydroquinone glucosides 325.6 mM (88.6 g/l), resorcinol glucosides 130.2 mM (35.4 g/l) and catechol glucosides 284.4 mM (77.4 g/l) when 400 mM hydroquinone, 200 mM resorcinol and 300 mM catechol, respectively, were used as an acceptor substrate. Furthermore, the use of commercially available amyloglucosidase at the end of the transglycosylation reaction minimized the glucooligosaccharides, thereby enhancing the target productivity of mono-glucosides. Moreover, the immobilized DgAS on Amicogen LKZ118 beads led to a 278.4 mM (75.8 g/l), 108.8 mM (29.6 g/l) and 211.2 mM (57.5 g/l) final concentration of mono-glycosylated product of hydroquinone, catechol and resorcinol at 35 cycles, respectively, when the same substrate concentration was used as mentioned above. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% during 35 cycles of reactions in an immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. The immobilized DgAS enhanced the efficiency of the glycosylation reaction and is therefore considered effective for industrial application.
Abstract
The amylosucrase encoding gene from Deinococcus geothermalis DSM 11300 (DgAS) was codonoptimized and expressed in Escherichia coli. The enzyme was employed for biosynthesis of three different dihydroxybenzene glucosides using sucrose as the source of glucose moiety. The reaction parameters, including temperature, pH, and donor (sucrose) and acceptor substrate concentrations, were optimized to increase the production yield. This study demonstrates the highest ever reported molar yield of hydroquinone glucosides 325.6 mM (88.6 g/l), resorcinol glucosides 130.2 mM (35.4 g/l) and catechol glucosides 284.4 mM (77.4 g/l) when 400 mM hydroquinone, 200 mM resorcinol and 300 mM catechol, respectively, were used as an acceptor substrate. Furthermore, the use of commercially available amyloglucosidase at the end of the transglycosylation reaction minimized the glucooligosaccharides, thereby enhancing the target productivity of mono-glucosides. Moreover, the immobilized DgAS on Amicogen LKZ118 beads led to a 278.4 mM (75.8 g/l), 108.8 mM (29.6 g/l) and 211.2 mM (57.5 g/l) final concentration of mono-glycosylated product of hydroquinone, catechol and resorcinol at 35 cycles, respectively, when the same substrate concentration was used as mentioned above. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% during 35 cycles of reactions in an immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. The immobilized DgAS enhanced the efficiency of the glycosylation reaction and is therefore considered effective for industrial application.
참고문헌 (38)
- 김묘덕, "Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives", Journal of Microbiology and Biotechnology, 26(11), pp.1845~1854 (2016), 한국미생물·생명공학회
- Overwin H, "Flavanone and isoflavone glucosylation by non-Leloir glycosyltransferases", J. Biotechnol., 233, pp.121~128 (2016)[DOI]
- Liang C, "Engineering a carbohydrate-processing transglycosidase into glycosyltransferase for natural product glycodiversification", Sci. Rep., 6, pp.21051~ (2016)[DOI]
- Lim M-C, "Amylosucrase-mediated synthesis and self-assembly of amylose magnetic microparticles", RSC Adv., 5, pp.36088~36091 (2015)[DOI]
- Letona CAM, "Amylosucrase-mediated beta-carotene encapsulation in amylose microparticles", Biotechnol. Prog., 33, pp.1640~1646 (2017)[DOI]
- O'Neill EC, "Sugar-coated sensor chip and nanoparticle surfaces for the in vitro enzymatic synthesis of starch-like materials", Chem. Sci., 5, pp.341~350 (2014)[DOI]
- Smit N, "The hunt for natural skin-whitening agents", Int. J. Mol. Sci., 10, pp.5326~5349 (2009)[DOI]
- Boer J, "Resorcinol peels as a possible self-treatment of painful nodules in hidradenitis suppurativa", Clin. Exp. Dermatol., 35, pp.36~40 (2010)[DOI]
- Limsuwan T, "Ethosomes of phenylethyl resorcinol as vesicular delivery system for skin- lightening applications", BioMed. Res. Int., 83, pp.8310979~ (2017)
- Kim BS, "The improvement of skin- whitening of phenylethylr-Resorcinol by nanostructured lipid carriers", Nanomaterials, 7, pp.241~ (2017)[DOI]
- Jung CT, "In vitro and in vivo percutaneous absorption of catechol", Food Chem. Toxicol., 41, pp.885~895 (2003)[DOI]
- Zhang P, "Enhanced chemical and biological activities of a newly biosynthesized eugenol glycoconjugate, eugenol alpha-D-glucopyranoside", Appl. Microbiol. Biotechnol., 97, pp.1043~1050 (2013)[DOI]
- Seo DH, "High-yield enzymatic bioconversion of hydroquinone to alpha-arbutin, a powerful skin- lightening agent, by amylosucrase", Appl. Microbiol. Biotechnol., 94, pp.1189~1197 (2012)[DOI]
- Lu L, "Glycosylation of phenolic compounds by the site-mutated beta-galactosidase from Lactobacillus bulgaricus L3", PLoS One, 10, pp.e0121445~ (2015)[DOI]
- Parajuli P, "Enzymatic synthesis of epothilone A glycosides", AMB Express, 4, pp.31~ (2014)[DOI]
- Pandey RP, "Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids", Carbohyd. Res., 393, pp.26~31 (2014)[DOI]
- Guerin F, "Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis", J. Biol. Chem., 287, pp.6642~6654 (2012)[DOI]
- Selmi B, "Amyloglucosidase hydrolysis of high-pressure and thermally- gelatinized corn and wheat starches", J. Agric. Food Chem., 48, pp.2629~2633 (2000)[DOI]
- Garcia-Salas P, "Phenolic-compound-extraction systems for fruit and vegetable samples", Molecules, 15, pp.8813~8826 (2010)[DOI]
- Suzuki Y, "Enzymatic Glycosylation of Aglycones of Pharmacological Significance;Carbohydrate Biotechnology Protocols", pp.297~312 (1999), Humana Press
- Cho HK, "Biosynthesis of (+)-catechin glycosides using recombinant amylosucrase from Deinococcus geothermalis DSM 11300", Enzyme Microb. Technol., 49, pp.246~253 (2011)[DOI]
- Li D, "Glycosylation of genistin into soluble inclusion complex form of cyclic glucans by enzymatic modification", J. Agric. Food Chem., 53, pp.6516~6524 (2005)[DOI]
- Park H, "Enzymatic synthesis of piceid glucosides using maltosyltransferase from Caldicellulosiruptor bescii DSM 6725", J. Agric. Food Chem., 60, pp.8183~8189 (2012)[DOI]
- Seo DH, "High-yield enzymatic bioconversion of hydroquinone to alpha-arbutin, a powerful skin- lightening agent, by amylosucrase", Appl. Microbiol. Biotechnol., 94, pp.1189~1197 (2012)[DOI]
- Bae HK, "Modification of ascorbic acid using transglycosylation activity of Bacillus stearothermophilus maltogenic amylase to enhance its oxidative stability", J. Agric. Food Chem., 50, pp.3309~3316 (2002)[DOI]
- Rowan AS, "Recent developments in preparative enzymatic syntheses of carbohydrates", Nat. Prod. Rep., 23, pp.412~443 (2006)[DOI]
- Thibodeaux CJ, "Unusual sugar biosynthesis and natural product glycodiversification", Nature, 446, pp.1008~1016 (2007)[DOI]
- Wang LX, "Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation", Carbohydr. Res., 343, pp.1509~1522 (2008)[DOI]
- Liu C, "Toward a cost-effective method for <TEX>${\alpha}$<", TEX>-arbutin production by using immobilized hydroquinone as a glucosyl acceptor, 2013, pp.48, 1447~1452
- Yao RS, "Degradation of phenolic compounds with hydrogen peroxide catalyzed by enzyme from Serratia marcescens AB 90027", Water Res., 40, pp.3091~3098 (2006)[DOI]
- Yu S, "Highly efficient biosynthesis of <TEX>${\alpha}$<", TEX>-arbutin from hydroquinone by an amylosucrase from Cellulomonas carboniz, 2018, pp.68, 93~99
- Bryjak J, "Immobilization of lipase and penicillin acylase on hydrophobic acrylic carriers", Enzyme Microb. Technol., 39, pp.573~578 (2006)[DOI]
- Kim TS, "A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization", Sci. Rep., 6, pp.33438~ (2016)[DOI]
- Hernaiz MJ, "Immobilization", stabilization on Eupergit C of the beta-galactosidase from B. circulans and an alpha-galactosidase from Aspergillus oryzae, 2000, pp.27, 26~32
- Katchalski-Katzir E, "Eupergit<TEX>$^{(R)}$<", TEX> C, a carrier for immobilization of enzymes of industrial potential, 2000, pp.10, 157~176
- Boller T, "EUPERGIT oxirane acrylic beads: how to make enzymes fit for biocatalysis", Organ. Process Res. Dev., 6, pp.509~519 (2002)[DOI]
- Melander WR, "Salt-mediated retention of proteins in hydrophobic-interaction chromatography: application of solvophobic theory", J. Chromatography, 317, pp.67~85 (1984)[DOI]
- Wheatley JB, "Salt-induced immobilization of affinity ligands onto epoxide-activated supports", J. Chromatography A, 849, pp.1~12 (1999)[DOI]