Application of Cyclodextrin Glucosyltransferase in the Glycosylation Modification of Natural Products

doi:10.13560/j.cnki.biotech.bull.1985.2021-0642

Abstract

Abstract:

Cyclodextrin glucosyltransferase（CGTase）is a kind of α-amylase that can catalyze the cleavage and cyclization of α-1, 4 bonds in starch or polysaccharides to form cyclodextrins（CDs）. CGTase is mainly used in industry to produce cyclodextrins. In recent years,There has been remarkable progress in the use of the transglycosylation effect of CGTase to modify the properties of natural products,which is becoming a promising development direction. This review introduces the source,protein structure and catalytic mechanism of CGTase,and focuses on its application in glycosylation modification of natural products in recent years,aiming to provide references for the in-depth research and application of CGTase in this field.

Key words: cyclodextrin glucosyltransferase, protein structure, natural products, glycosylation reaction

ZHANG Guo-ning, FENG Jing-xian, YANG Ying-bo, CHEN Wan-sheng, XIAO Ying. Application of Cyclodextrin Glucosyltransferase in the Glycosylation Modification of Natural Products[J]. Biotechnology Bulletin, 2022, 38(3): 246-255.

Figures/Tables 7

References 69

[1]	van de Manakker F, Vermonden T, van Nostrum CF, et al. Cyclodextrin-based polymeric materials:synjournal, properties, and pharmaceutical/biomedical applications[J]. Biomacromolecules, 2009, 10(12):3157-3175. doi: 10.1021/bm901065f pmid: 19921854
[2]	Biwer A, Antranikian G, Heinzle E. Enzymatic production of cyclodextrins[J]. Appl Microbiol Biotechnol, 2002, 59(6):609-617. pmid: 12226716
[3]	Sonnendecker C, Zimmermann W. Change of the product specificity of a cyclodextrin glucanotransferase by semi-rational mutagenesis to synthesize large-ring cyclodextrins[J]. Catalysts, 2019, 9(3):242. doi: 10.3390/catal9030242 URL
[4]	Han R, Li J, Shin HD, et al. Recent advances in discovery, heterologous expression, and molecular engineering of cyclodextrin glycosyltransferase for versatile applications[J]. Biotechnol Adv, 2014, 32(2):415-428. doi: 10.1016/j.biotechadv.2013.12.004 URL
[5]	Leemhuis H, Kelly RM, Dijkhuizen L. Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications[J]. Appl Microbiol Biotechnol, 2010, 85(4):823-835. doi: 10.1007/s00253-009-2221-3 pmid: 19763564
[6]	Kim MH, Sohn CB, Oh TK. Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli[J]. FEMS Microbiol Lett, 1998, 164(2):411-418. pmid: 9682490
[7]	Nazir S, Sulistyo J, Hashmi MI, et al. Enzymatic synjournal of polyphenol glycosides catalyzed by transglycosylation reaction of cyclodextrin glucanotransferase derived from Trichoderma viride[J]. J Food Sci Technol, 2018, 55(8):3026-3034. doi: 10.1007/s13197-018-3223-x URL
[8]	Bautista V, Esclapez J, Pérez-Pomares F, et al. Cyclodextrin glycosyltransferase:a key enzyme in the assimilation of starch by the halophilic archaeon Haloferax mediterranei[J]. Extremophiles, 2012, 16(1):147-159. doi: 10.1007/s00792-011-0414-z pmid: 22134680
[9]	Lim CH, Rasti B, Sulistyo J, et al. Comprehensive study on transglycosylation of CGTase from various sources[J]. Heliyon, 2021, 7(2):e06305. doi: 10.1016/j.heliyon.2021.e06305 URL
[10]	Tachibana Y, Kuramura A, Shirasaka N, et al. Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp[J]. Appl Environ Microbiol, 1999, 65(5):1991-1997. doi: 10.1128/AEM.65.5.1991-1997.1999 URL
[11]	Svensson B. Protein engineering in the alpha-amylase family:catalytic mechanism, substrate specificity, and stability[J]. Plant Mol Biol, 1994, 25(2):141-157. pmid: 8018865
[12]	Klein C, Schulz GE. Structure of cyclodextrin glycosyltransferase refined at 2. 0 A resolution[J]. J Mol Biol, 1991, 217(4):737-750. pmid: 1826034
[13]	Wind RD, Buitelaar RM, Dijkhuizen L. Engineering of factors determining alpha-amylase and cyclodextrin glycosyltransferase specificity in the cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1[J]. Eur J Biochem, 1998, 253(3):598-605. pmid: 9654055
[14]	Janeček Š. Parallel β/α-barrels of α-amylase, cyclodextrin glycosyltransferase and oligo-1, 6-glucosidase versus the barrel of β-amylase:Evolutionary distance is a reflection of unrelated sequences[J]. FEBS Lett, 1994, 353(2):119-123. doi: 10.1016/0014-5793(94)01019-6 URL
[15]	Sonnendecker C, Zimmermann W. Domain shuffling of cyclodextrin glucanotransferases for tailored product specificity and thermal stability[J]. FEBS Open Bio, 2019, 9(2):384-395. doi: 10.1002/2211-5463.12588 pmid: 30761262
[16]	Leemhuis H, Rozeboom HJ, Dijkstra BW, et al. Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge[J]. Proteins, 2004, 54(1):128-134. doi: 10.1002/prot.10516 URL
[17]	Knegtel RM, Strokopytov B, Penninga D, et al. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products[J]. J Biol Chem, 1995, 270(49):29256-29264. doi: 10.1074/jbc.270.49.29256 pmid: 7493956
[18]	Rimphanitchayakit V, Tonozuka T, Sakano Y. Construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity[J]. Carbohydr Res, 2005, 340(14):2279-2289. doi: 10.1016/j.carres.2005.07.013 URL
[19]	Zhou J, Feng Z, Liu S, et al. CGTase, a novel antimicrobial protein from Bacillus cereus YUPP-10, suppresses Verticillium dahliae and mediates plant defence responses[J]. Mol Plant Pathol, 2021, 22(1):130-144. doi: 10.1111/mpp.13014 URL
[20]	Li Z, Huang M, Gu Z, et al. Asp577 mutations enhance the catalytic efficiency of cyclodextrin glycosyltransferase from Bacillus circulans[J]. Int J Biol Macromol, 2016, 83:111-116. doi: 10.1016/j.ijbiomac.2015.11.042 URL
[21]	Wang L, Duan XG, Wu J. Enhancing the α-cyclodextrin specificity of cyclodextrin glycosyltransferase from Paenibacillus macerans by mutagenesis masking subsite -7[J]. Appl Environ Microbiol, 2016, 82(8):2247-2255. doi: 10.1128/AEM.03535-15 URL
[22]	Li ZF, Ban XF, Gu ZB, et al. Mutations enhance β-cyclodextrin specificity of cyclodextrin glycosyltransferase from Bacillus circulans[J]. Carbohydr Polym, 2014, 108:112-117. doi: 10.1016/j.carbpol.2014.03.015 URL
[23]	Chen FJ, Xie T, Yue Y, et al. Molecular dynamic analysis of mutant Y195I α-cyclodextrin glycosyltransferase with switched product specificity from α-cyclodextrin to γ-cyclodextrin[J]. J Mol Modeling, 2015, 21(8):1-9. doi: 10.1007/s00894-014-2561-5 URL
[24]	Tao X, Wang T, Su L, et al. Enhanced 2- o-alpha-d-glucopyranosyl-l-ascorbic acid synjournal through iterative saturation mutagenesis of acceptor subsite residues in Bacillus stearothermophilus NO₂ cyclodextrin glycosyltransferase. J Agric Food Chem[J], 2018, 66(34):9052-9060.
[25]	Han R, Liu L, Shin HD, et al. Iterative saturation mutagenesis of -6 subsite residues in cyclodextrin glycosyltransferase from Paenibacillus macerans to improve maltodextrin specificity for 2-O-D-glucopyranosyl-L-ascorbic acid synjournal[J]. Appl Environ Microbiol, 2013, 79(24):7562-7568. doi: 10.1128/AEM.02918-13 URL
[26]	Gudiminchi RK, Towns A, Varalwar S, et al. Enhanced synjournal of 2-O-α-d-glucopyranosyl-l-ascorbic acid from α-cyclodextrin by a highly disproportionating CGTase[J]. ACS Catal, 2016, 6(3):1606-1615. doi: 10.1021/acscatal.5b02108 URL
[27]	Uitdehaag JCM, van der Veen BA, Dijkhuizen L, et al. Catalytic mechanism and product specificity of cyclodextrin glycosyltransferase, a prototypical transglycosylase from the α-amylase family[J]. Enzyme Microb Technol, 2002, 30(3):295-304. doi: 10.1016/S0141-0229(01)00498-7 URL
[28]	Strokopytov B, Penninga D, Rozeboom HJ, et al. X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. implications for the catalytic mechanism of glycosidases[J]. Biochemistry, 1995, 34(7):2234-2240. pmid: 7857935
[29]	Uitdehaag JC, Mosi R, Kalk KH, et al. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family[J]. Nat Struct Biol, 1999, 6(5):432-436. pmid: 10331869
[30]	Choung WJ, Hwang SH, Ko DS, et al. Enzymatic synjournal of a novel kaempferol-3-O-β-d-glucopyranosyl-(1→4)-O-α-d-glucopyranoside using cyclodextrin glucanotransferase and its inhibitory effects on aldose reductase, inflammation, and oxidative stress[J]. J Agric Food Chem, 2017, 65(13):2760-2767. doi: 10.1021/acs.jafc.7b00501 URL
[31]	Marié T, Willig G, Teixeira ARS, et al. Enzymatic synjournal of resveratrol α-glycosides from β-cyclodextrin-resveratrol complex in water[J]. ACS Sustainable Chem Eng, 2018, 6(4):5370-5380. doi: 10.1021/acssuschemeng.8b00176 URL
[32]	Radu O L, Armand S, Lenouvel F. La glycosylation de la luteoline, en milieux de solventes organiques, par l’action catalytique de la cyclodextrine glycosyltransferase de Bacillus circulans. Revue Roumaine de Chimie[J], 2006, 51(2):147-152.
[33]	Kometani T, Nishimura T, Nakae T, et al. Synjournal of neohesperidin glycosides and naringin glycosides by cyclodextrin glucanotransferase from an alkalophilic Bacillus species[J]. Biosci Biotechnol Biochem, 1996, 60(4):645-649. doi: 10.1271/bbb.60.645 URL
[34]	Suzuki Y, Suzuki K. Enzymatic formation of 4G-alpha-D-glucopyranosyl-rutin[J]. Agric Biol Chem, 1991, 55(1):181-187. pmid: 1368662
[35]	Markosyan AA, Abelyan LA, Markosyan AI, et al. Transglycosylation of benzo[h]quinazolines[J]. Appl Biochem Microbiol, 2009, 45(2):130-136. doi: 10.1134/S0003683809020033 URL
[36]	Han RZ, Ni J, Zhou JY, et al. Engineering of cyclodextrin glycosyltransferase reveals pH-regulated mechanism of enhanced long-chain glycosylated sophoricoside specificity[J]. Appl Environ Microbiol, 2020, 86(7):e00004-20.
[37]	Lee YS, Woo JB, Ryu SI, et al. Glucosylation of flavonol and flavanones by Bacillus cyclodextrin glucosyltransferase to enhance their solubility and stability[J]. Food Chem, 2017, 229:75-83. doi: 10.1016/j.foodchem.2017.02.057 URL
[38]	Aramsangtienchai P, Chavasiri W, Ito K, et al. Synjournal of epicatechin glucosides by a β-cyclodextrin glycosyltransferase[J]. J Mol Catal B:Enzym, 2011, 73(1/2/3/4):27-34. doi: 10.1016/j.molcatb.2011.07.013 URL
[39]	Gonzalez-Alfonso JL, Leemans L, Poveda A, et al. Efficient α-glucosylation of epigallocatechin gallate catalyzed by cyclodextrin glucanotransferase from Thermoanaerobacter species[J]. J Agric Food Chem, 2018, 66(28):7402-7408. doi: 10.1021/acs.jafc.8b02143 URL
[40]	Kometani T, Terada Y, Nishimura T, et al. Transglycosylation to hesperidin by cyclodextrin glucanotransferase from an alkalophilic Bacillus species in alkaline pH and properties of hesperidin glycosides[J]. Biosci Biotechnol Biochem, 1994, 58(11):1990-1994. doi: 10.1271/bbb.58.1990 URL
[41]	Huang W, He Q, Zhou ZR, et al. Enzymatic synjournal of puerarin glucosides using cyclodextrin glucanotransferase with enhanced antiosteoporosis activity[J]. ACS Omega, 2020, 5(21):12251-12258. doi: 10.1021/acsomega.0c00950 pmid: 32548408
[42]	Sugimoto K, Nishimura T, Nomura K, et al. Syntheses of arbutin-alpha-glycosides and a comparison of their inhibitory effects with those of alpha-arbutin and arbutin on human tyrosinase[J]. Chem Pharm Bull:Tokyo, 2003, 51(7):798-801. doi: 10.1248/cpb.51.798 URL
[43]	Shimoda K, Akagi M, Hamada H. Production of β-maltooligosaccharides of α- and δ-tocopherols by Klebsiella pneumoniae and cyclodextrin glucanotransferase as anti-allergic agents[J]. Molecules, 2009, 14(8):3106-3114. doi: 10.3390/molecules14083106 pmid: 19701147
[44]	Mathew S, Adlercreutz P. Regioselective glycosylation of hydroquinone to α-arbutin by cyclodextrin glucanotransferase from Thermoanaerobacter sp[J]. Biochem Eng J, 2013, 79:187-193. doi: 10.1016/j.bej.2013.08.001 URL
[45]	Kitao S, Sekine H. Α-D-glucosyl transfer to phenolic compounds by sucrose phosphorylase from Leuconostoc mesenteroides and production of α-arbutin[J]. Biosci Biotechnol Biochem, 1994, 58(1):38-42. doi: 10.1271/bbb.58.38 URL
[46]	Urbach C, Halila S, Guerreiro C, et al. CGTase-catalysed Cis-glucosylation of L-rhamnosides for the preparation of Shigella flexneri 2a and 3a haptens[J]. Chembiochem, 2014, 15(2):293-300. doi: 10.1002/cbic.201300597 URL
[47]	Funayama M, Nishino T, Hirota A, et al. Enzymatic synjournal of(+)catechin-α-glucoside and its effect on tyrosinase activity[J]. Biosci Biotechnol Biochem, 1993, 57(10):1666-1669. doi: 10.1271/bbb.57.1666 URL
[48]	Okada K, Zhao HS, Izumi M, et al. Glucosylation of sucrose laurate with cyclodextrin glucanotransferase[J]. Biosci Biotechnol Biochem, 2007, 71(3):826-829. doi: 10.1271/bbb.60646 URL
[49]	Shimoda K, Hamada H. Production of hesperetin glycosides by Xanthomonas campestris and cyclodextrin glucanotransferase and their anti-allergic activities[J]. Nutrients, 2010, 2(2):171-180. doi: 10.3390/nu2020171 pmid: 22254014
[50]	Shimoda K, Kubota N, Akagi M. Synjournal of capsaicin oligosaccharides and their anti-allergic activity—synjournal of capsaicin oligosaccharides as anti-allergic food-additives[J]. Adv Chem Eng Sci, 2012, 2(1):45-49. doi: 10.4236/aces.2012.21006 URL
[51]	Torres P, Poveda A, Jimenez-Barbero J, et al. Enzymatic synjournal of α-glucosides of resveratrol with surfactant activity[J]. Adv Synth Catal, 2011, 353(7):1077-1086. doi: 10.1002/adsc.201000968 URL
[52]	Yoon SH, Bruce Fulton D, Robyt JF. Enzymatic synjournal of two salicin analogues by reaction of salicyl alcohol with Bacillus macerans cyclomaltodextrin glucanyltransferase and Leuconostoc mesenteroides B-742CB dextransucrase[J]. Carbohydr Res, 2004, 339(8):1517-1529. doi: 10.1016/j.carres.2004.03.018 URL
[53]	Yoshinaga K, Abe J, Tanimoto T, et al. Preparation and reactivity of a novel disaccharide, glucosyl 1, 5-anhydro-D-fructose(1, 5-anhydro-3-O-alpha-glucopyranosyl-D-fructose)[J]. Carbohydr Res, 2003, 338(21):2221-2225. doi: 10.1016/S0008-6215(03)00341-0 URL
[54]	Yoshinaga K, Abe J, Tanimoto T, et al. Preparation and reactivity of a novel disaccharide, glucosyl 1, 5-anhydro-D-fructose(1, 5-anhydro-3-O-alpha-glucopyranosyl-D-fructose)[J]. Carbohydr Res, 2003, 338(21):2221-2225. doi: 10.1016/S0008-6215(03)00341-0 URL
[55]	Miranda-Molina A, Marquina-Bahena S, López-Munguía A, et al. Regioselective glucosylation of inositols catalyzed by Thermoanaerobacter sp. CGTase[J]. Carbohydr Res, 2012, 360:93-101. doi: 10.1016/j.carres.2012.08.002 URL
[56]	Jaitak V, Kaul VK, Bandna, et al. Simple and efficient enzymatic transglycosylation of stevioside by β-cyclodextrin glucanotransferase from Bacillus firmus[J]. Biotechnol Lett, 2009, 31(9):1415-1420. doi: 10.1007/s10529-009-0020-7 pmid: 19466564
[57]	Abelyan VA, Balayan AM, Ghochikyan VT, et al. Transglycosylation of stevioside by cyclodextrin glucanotransferases of various groups of microorganisms[J]. Appl Biochem Microbiol, 2004, 40(2):129-134. doi: 10.1023/B:ABIM.0000018914.08571.50 URL
[58]	Yu XJ, Yang JS, Li BZ, et al. High efficiency transformation of stevioside into a single mono-glycosylated product using a cyclodextrin glucanotransferase from Paenibacillus sp. CGMCC 5316[J]. World J Microbiol Biotechnol, 2015, 31(12):1983-1991. doi: 10.1007/s11274-015-1947-6 URL
[59]	Kim YH, Lee YG, Choi KJ, et al. Transglycosylation to ginseng saponins by cyclomaltodextrin glucanotransferases[J]. Biosci Biotechnol Biochem, 2001, 65(4):875-883. doi: 10.1271/bbb.65.875 URL
[60]	Ohtani K, Aikawa Y, Ishikawa H, et al. Further study on the 1, 4-. ALPHA. -transglucosylation of rubusoside, a sweet steviol-bisglucoside from Rubus suavissimus[J]. Agric Biol Chem, 1991, 55(2):449-453. pmid: 1368695
[61]	Muñoz-Labrador A, Azcarate S, Lebrón-Aguilar R, et al. High-yield synjournal of transglycosylated mogrosides improves the flavor profile of monk fruit extract sweeteners[J]. J Agric Food Chem, 2021, 69(3):1011-1019. doi: 10.1021/acs.jafc.0c07267 URL
[62]	Yoshikawa S, Murata Y, Sugiura M, et al. Transglycosylation of mogroside V, a triterpene glycoside in Siraitia grosvenori, by cyclodextrin glucanotransferase and improvement of the qualities of sweetness[J]. J Appl Glycosci, 2005, 52(3):247-252. doi: 10.5458/jag.52.247 URL
[63]	Nakano H, Kiso T, Okamoto K, et al. Synjournal of glycosyl glycerol by cyclodextrin glucanotransferases[J]. J Biosci Bioeng, 2003, 95(6):583-588. doi: 10.1016/S1389-1723(03)80166-4 URL
[64]	Han R, Liu L, Shin HD, et al. Site-saturation engineering of lysine 47 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance substrate specificity towards maltodextrin for enzymatic synjournal of 2-O-D-glucopyranosyl-L-ascorbic acid(AA-2G)[J]. Appl Microbiol Biotechnol, 2013, 97(13):5851-5860. doi: 10.1007/s00253-012-4514-1 URL
[65]	Han RZ, Liu L, Li JH, et al. Functions, applications and production of 2-O-d-glucopyranosyl-l-ascorbic acid[J]. Appl Microbiol Biotechnol, 2012, 95(2):313-320. doi: 10.1007/s00253-012-4150-9 URL
[66]	Martı́n MT, Angeles Cruces M, Alcalde M, et al. Synjournal of maltooligosyl fructofuranosides catalyzed by immobilized cyclodextrin glucosyltransferase using starch as donor[J]. Tetrahedron, 2004, 60(3):529-534. doi: 10.1016/j.tet.2003.10.113 URL
[67]	Moon S, Lee H, Mathiyalagan R, et al. Synjournal of a novel α-glucosyl ginsenoside F1 by cyclodextrin glucanotransferase and its in vi-tro cosmetic applications[J]. Biomolecules, 2018, 8(4):142. doi: 10.3390/biom8040142 URL
[68]	Tao XM, Su LQ, Wang L, et al. Improved production of cyclodextrin glycosyltransferase from Bacillus stearothermophilus NO₂ in Escherichia coli via directed evolution[J]. Appl Microbiol Biotechnol, 2020, 104(1):173-185. doi: 10.1007/s00253-019-10249-8 URL
[69]	Chen S, Xiong Y, Su L, et al. Position 228 in Paenibacillus macerans cyclodextrin glycosyltransferase is critical for 2-O-d-glucopyranosyl-l-ascorbic acid synjournal[J]. J Biotechnol, 2017, 247:18-24. doi: 10.1016/j.jbiotec.2017.02.011 URL

底物 Substrate	结构类型 Structure type	CGTase来源 CGTase source	糖基供体 Glycosyl donor	糖苷化产物应用 Application of glycosylation products	参考文献 Reference
木犀草素	黄酮类	Bacillus circulans	α-环糊精	水溶性增加,增强了其在医疗实践中的应用	[32]
柚皮苷	黄酮类	Alkalophilic Bacillus sp	麦芽煳精	溶解度提高1.0×10³倍,扩大其在食品工业中的应用范围	[33]
新橙皮苷	黄酮类	Alkalophilic Bacillus	β-环糊精	溶解度提高1.5×10³倍,扩大其在食品工业中的应用范围	[33]
芦丁	黄酮醇类	Bacillus macerans	糊精	溶解度提高3×10⁴倍	[34]
苯并[H]喹唑啉类化合物	杂环化合物	Thermophilic Bacterial	γ-环糊精	增高水溶性,提高制剂生物活性和生物利用度	[35]
槐糖苷	异黄酮类	Paenibacillus macerans	α-环糊精或麦芽糖	糖链增长水溶性增加,扩大在食品和制药行业中的应用范围	[36]
槲皮素-3-葡萄糖;低聚葡萄糖基柚皮素-7-葡萄糖;低聚葡萄糖基橙皮素-7-葡萄糖	黄酮醇、二氢黄酮	B. macerans	α-环糊精 α-cyclodextrin	糖苷产物水溶性增强,扩大在食品和制药行业中的应用范围	[37]
（-）-表儿茶素（EC）	黄烷-3醇类	Paenibacillus sp.	β-环糊精（最佳）;淀粉;麦芽七糖（G7）	糖苷产物水溶性增强,扩大在食品行业中的应用范围	[38]
没食子儿茶素没食子酸（EGCG）	黄烷-3醇类	Thermoanaerobacter sp	淀粉	植物多酚糖基化,提高溶解度和生物利用度	[39]
橙皮苷	二氢黄酮	A. Bacillus	可溶性淀粉	水溶性提高300倍,扩大应用范围	[40]
葛根素	异黄酮	Bacillus licheniformis	α-cyclodextrin	PU-G、PU-2G以及PU-3G与PU相比,溶解度分别增强16.5、100.9和179.1倍	[41]

底物 Substrate	结构类型 Structure type	CGTase来源 CGTase source	糖基供体 Glycosyl donor	糖苷化产物应用 Application of glycosylation products	参考文献 Reference
木犀草素	黄酮类	Bacillus circulans	α-环糊精	水溶性增加,增强了其在医疗实践中的应用	[32]
柚皮苷	黄酮类	Alkalophilic Bacillus sp	麦芽煳精	溶解度提高1.0×10³倍,扩大其在食品工业中的应用范围	[33]
新橙皮苷	黄酮类	Alkalophilic Bacillus	β-环糊精	溶解度提高1.5×10³倍,扩大其在食品工业中的应用范围	[33]
芦丁	黄酮醇类	Bacillus macerans	糊精	溶解度提高3×10⁴倍	[34]
苯并[H]喹唑啉类化合物	杂环化合物	Thermophilic Bacterial	γ-环糊精	增高水溶性,提高制剂生物活性和生物利用度	[35]
槐糖苷	异黄酮类	Paenibacillus macerans	α-环糊精或麦芽糖	糖链增长水溶性增加,扩大在食品和制药行业中的应用范围	[36]
槲皮素-3-葡萄糖;低聚葡萄糖基柚皮素-7-葡萄糖;低聚葡萄糖基橙皮素-7-葡萄糖	黄酮醇、二氢黄酮	B. macerans	α-环糊精 α-cyclodextrin	糖苷产物水溶性增强,扩大在食品和制药行业中的应用范围	[37]
（-）-表儿茶素（EC）	黄烷-3醇类	Paenibacillus sp.	β-环糊精（最佳）;淀粉;麦芽七糖（G7）	糖苷产物水溶性增强,扩大在食品行业中的应用范围	[38]
没食子儿茶素没食子酸（EGCG）	黄烷-3醇类	Thermoanaerobacter sp	淀粉	植物多酚糖基化,提高溶解度和生物利用度	[39]
橙皮苷	二氢黄酮	A. Bacillus	可溶性淀粉	水溶性提高300倍,扩大应用范围	[40]
葛根素	异黄酮	Bacillus licheniformis	α-cyclodextrin	PU-G、PU-2G以及PU-3G与PU相比,溶解度分别增强16.5、100.9和179.1倍	[41]

底物 Substrate	结构类型 Structure type	CGTase来源 CGTase source	糖基供体 Glycosyl donor	糖苷化产物应用 Application of glycosylation products	参考文献 Reference
熊果苷arbutin	苯酚类	Bacillus macerans	淀粉	对人酪氨酸酶抑制活性增强	[42]
α-生育酚-β-葡萄糖苷、δ-生育酚-β-葡萄糖苷	多酚类	不明确	淀粉	对大鼠腹膜肥大细胞产生IgE抗体和增强组胺释放抑制作用	[43]
对苯二酚（HQ）	苯酚类	Thermoanaerobacter sp	麦芽糊精	抗褐变能力增强	[44-45]
α-L-鼠李糖	糖类	Bacillus circulans 251	麦芽糖糊精	可能应用于针对细菌性痢疾的合成候选疫苗	[46]
槲皮素-3-葡萄糖;低聚葡萄糖基柚皮素-7-葡萄糖;低聚葡萄糖基橙皮素-7-葡萄糖	黄酮醇、二氢黄酮	B. macerans	α-环糊精	对Cu²⁺氧化降解的抵抗能力大大增强	[37]
（+）儿茶素	黄烷-3醇类	B. macerans	淀粉	抑制蘑菇中酪氨酸酶的活性	[47]
辣木提取物中的多酚类化合物	多酚类	Trichoderma viride	小麦淀粉	抗氧化和清除自由基能力增强	[7]
月桂酸蔗糖	糖类	不明确	糊精	潜在的抗肿瘤和杀虫活性	[48]
橙皮素苷（3'-, 5-,and 7-O-glucosides）	二氢黄酮	不明确	淀粉	对IgE抗体和大鼠嗜中性白细胞产生O₂具有抑制作用	[49]
辣椒素的β葡萄糖苷	芳香烃类	不明确	淀粉	抑制IgE抗体的形成	[50]
白藜芦醇	多酚类	Thermoanaerobacter sp	淀粉	具有表面活性剂性质	[51]
水杨醇	酚类	B. macerans	α-环糊精	促进吸收,并可作为温和有效的解热镇痛药前体	[52]
（-）-表儿茶素（EC）	黄烷-3醇类	Paenibacillus sp.	β-环糊精（最佳）;淀粉;麦芽七糖（G7）	糖苷产物抗紫外线褐变能力增强	[38]
橙皮苷	二氢黄酮类	Alkalophilic Bacillus	可溶性淀粉	糖苷产物吸收紫外线以稳定食品中的色素	[40]
Anhydro-D-fructose	糖类	不明确	β-环糊精	降低了与牛血清白蛋白的氨基羰基反应活性	[53]
1, 5-Anhydro-D-fructose	糖类	Bacillus stearothermophilus	β-环糊精	为提高食物蛋白溶解性和稳定性以及蛋白酶抗性提供新的手段	[54]
D-pinitol L-chiro-inositol D-chiro-Inositol muco-inositol allo-inositol	脂环醇	Thermoanaerobacter sp	β-环糊精	肌醇糖基化衍生物在细胞功能中具有多种生理作用	[55]
肌醇（myoinositol）	脂环醇	Bacillus ohbensis.	β-环糊精	肌醇糖基化衍生物在细胞功能中具有多种生理作用	[55]

底物 Substrate	结构类型 Structure type	CGTase来源 CGTase source	糖基供体 Glycosyl donor	糖苷化产物应用 Application of glycosylation products	参考文献 Reference
熊果苷arbutin	苯酚类	Bacillus macerans	淀粉	对人酪氨酸酶抑制活性增强	[42]
α-生育酚-β-葡萄糖苷、δ-生育酚-β-葡萄糖苷	多酚类	不明确	淀粉	对大鼠腹膜肥大细胞产生IgE抗体和增强组胺释放抑制作用	[43]
对苯二酚（HQ）	苯酚类	Thermoanaerobacter sp	麦芽糊精	抗褐变能力增强	[44-45]
α-L-鼠李糖	糖类	Bacillus circulans 251	麦芽糖糊精	可能应用于针对细菌性痢疾的合成候选疫苗	[46]
槲皮素-3-葡萄糖;低聚葡萄糖基柚皮素-7-葡萄糖;低聚葡萄糖基橙皮素-7-葡萄糖	黄酮醇、二氢黄酮	B. macerans	α-环糊精	对Cu²⁺氧化降解的抵抗能力大大增强	[37]
（+）儿茶素	黄烷-3醇类	B. macerans	淀粉	抑制蘑菇中酪氨酸酶的活性	[47]
辣木提取物中的多酚类化合物	多酚类	Trichoderma viride	小麦淀粉	抗氧化和清除自由基能力增强	[7]
月桂酸蔗糖	糖类	不明确	糊精	潜在的抗肿瘤和杀虫活性	[48]
橙皮素苷（3'-, 5-,and 7-O-glucosides）	二氢黄酮	不明确	淀粉	对IgE抗体和大鼠嗜中性白细胞产生O₂具有抑制作用	[49]
辣椒素的β葡萄糖苷	芳香烃类	不明确	淀粉	抑制IgE抗体的形成	[50]
白藜芦醇	多酚类	Thermoanaerobacter sp	淀粉	具有表面活性剂性质	[51]
水杨醇	酚类	B. macerans	α-环糊精	促进吸收,并可作为温和有效的解热镇痛药前体	[52]
（-）-表儿茶素（EC）	黄烷-3醇类	Paenibacillus sp.	β-环糊精（最佳）;淀粉;麦芽七糖（G7）	糖苷产物抗紫外线褐变能力增强	[38]
橙皮苷	二氢黄酮类	Alkalophilic Bacillus	可溶性淀粉	糖苷产物吸收紫外线以稳定食品中的色素	[40]
Anhydro-D-fructose	糖类	不明确	β-环糊精	降低了与牛血清白蛋白的氨基羰基反应活性	[53]
1, 5-Anhydro-D-fructose	糖类	Bacillus stearothermophilus	β-环糊精	为提高食物蛋白溶解性和稳定性以及蛋白酶抗性提供新的手段	[54]
D-pinitol L-chiro-inositol D-chiro-Inositol muco-inositol allo-inositol	脂环醇	Thermoanaerobacter sp	β-环糊精	肌醇糖基化衍生物在细胞功能中具有多种生理作用	[55]
肌醇（myoinositol）	脂环醇	Bacillus ohbensis.	β-环糊精	肌醇糖基化衍生物在细胞功能中具有多种生理作用	[55]

底物 Substrate	结构类型 Structure type	CGTase来源 CGTase source	糖基供体 Glycosyl donor	糖苷化产物应用 Application of glycosylation products	参考文献 Reference
新橙皮苷	黄酮类	Alkalophilic Bacillus	可溶性淀粉	苦味降低10倍	[33]
Neohesperidin	Flavonoid		Soluble starch	10 times lower of bitterness
甜叶悬钩子苷	二萜类	Bacillus circulans	可溶性淀粉	甜度增加	[60]
Rubusoside	Diterpenoid		Soluble starch	Increased sweetness
罗汉果V Mogroside V	四环三萜类 Tetracyclic triterpenoid	Paenibacillus macerans Geobacillus sp. Thermoanaerobacter sp.	麦芽糊精 Maltodextrin	甜度增加 Increased sweetness	[61-62]
甘油 Glycerin	脂肪醇 Fatty alcohol	Geobacillus（Bacillus）stearothermophilus（效果较好 Good effect） Thermoanaerobacter sp.（效果较好 Good effect）Bacillus circulans	淀粉Starch	有望应用于食品以改善口感It is expected to be used to improve the taste of food	[63]