Research progress in the preparation and modification of sucrose isomerase

  • LI Min ,
  • SHANG Jixu ,
  • JIA Zhenhua ,
  • LOH Teck Peng ,
  • LIAO Aimei
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  • 1(College of Advanced Interdisciplinary Science and Technology, Henan University of Technology, Zhengzhou 450001, China)
    2(College of International Education, Henan University of Technology, Zhengzhou 450001, China)

Received date: 2024-02-17

  Revised date: 2024-05-17

  Online published: 2025-02-21

Abstract

Isomaltulose, as a novel type of functional sugar, possesses characteristics such as low calorie content, anti-caries properties, easy absorption, and slow digestion.It is a sugar substitute suitable for diabetics and obese individuals, and it has broad applications in the food, pharmaceutical, and cosmetic industries.At present, the main preparation methods of isomaltulose include chemical synthesis, plant transgenic techniques, microbial conversion, and enzyme conversion.Among these methods, enzyme conversion has emerged as a new research focus in recent years, primarily utilized for sucrose isomerase (SIase).This paper reviews the mutation breeding of enzyme-producing strains of sucrose isomerase, heterologous expression, molecular modification, and chemical modification of SIase in the preparation of isomaltulose.The aim is to offer guidance for the development of related research work and industrial production.

Cite this article

LI Min , SHANG Jixu , JIA Zhenhua , LOH Teck Peng , LIAO Aimei . Research progress in the preparation and modification of sucrose isomerase[J]. Food and Fermentation Industries, 2025 , 51(3) : 385 -394 . DOI: 10.13995/j.cnki.11-1802/ts.038887

References

[1] SCHIWECK H, MUNIR M, RAPP K M, et al.New developments in the use of sucrose as an industrial bulk chemical[J].Sugar Industry, 1990, 115(7):555-565.
[2] LIU L N, BILAL M, LUO H Z, et al.Studies on biological production of isomaltulose using sucrose isomerase:Current status and future perspectives[J].Catalysis Letters, 2021, 151(7):1868-1881.
[3] ZHANG D H, LI N, LOK S M, et al.Isomaltulose Synthase (PalI) of Klebsiella sp.lx3 crystal structure and implication of mechanism[J].Journal of Biological Chemistry, 2003, 278(37):35428-35434.
[4] MATTES R, KLEIN K, SCHIWECK H, et al. DNA's encoding sucrose isomerase and palatinase[P]. US19950374155,1998-07-28.
[5] LEE H C, KIM J H, KIM S Y, et al.Isomaltose production by modification of the fructose-binding site on the basis of the predicted structure of sucrose isomerase from “Protaminobacter rubrum”[J].Applied and Environmental Microbiology, 2008, 74(16):5183-5194.
[6] VÉRONÈSE T, PERLOT P.Mechanism of sucrose conversion by the sucrose isomerase of Serratia plymuthica ATCC 15928[J].Enzyme and Microbial Technology, 1999, 24(5-6):263-269.
[7] LI X, ZHAO C, AN Q, et al.Substrate induction of isomaltulose synthase in a newly isolated Klebsiella sp.LX3[J].Journal of Applied Microbiology, 2003, 95(3):521-527.
[8] WU L, BIRCH R G.Characterization of Pantoea dispersa UQ68 J:Producer of a highly efficient sucrose isomerase for isomaltulose biosynthesis[J].Journal of Applied Microbiology, 2004, 97(1):93-103.
[9] LEE G Y, JUNG J H, SEO D H, et al.Isomaltulose production via yeast surface display of sucrose isomerase from Enterobacter sp.FMB-1 on Saccharomyces cerevisiae[J].Bioresource Technology, 2011, 102(19):9179-9184.
[10] LI S, CAI H, QING Y J, et al.Cloning and characterization of a sucrose isomerase from Erwinia rhapontici NX-5 for isomaltulose hyperproduction[J].Applied Biochemistry and Biotechnology, 2011, 163(1):52-63.
[11] LIU L, YU S H, ZHAO W.A novel sucrose isomerase producing isomaltulose from Raoultella terrigena[J].Applied Sciences, 2021, 11(12):5521.
[12] NAGAI-MIYATA Y, TSUYUKI K I, SUGITANI T, et al.Isolation and characterization of a trehalulose-producing strain of Agrobacterium[J].Bioscience, Biotechnology, and Biochemistry, 1993, 57(12):2049-2053.
[13] RAVAUD S, ROBERT X, WATZLAWICK H, et al.Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization[J].Journal of Biological Chemistry, 2007, 282(38):28126-28136.
[14] SALVUCCI M E.Distinct sucrose isomerases catalyze trehalulose synthesis in whiteflies, Bemisia argentifolii, and Erwinia rhapontici[J].Comparative Biochemistry and Physiology Part B:Biochemistry and Molecular Biology, 2003, 135(2):385-395.
[15] WU L G, BIRCH R G.Characterization of the highly efficient sucrose isomerase from Pantoea dispersa UQ68 J and cloning of the sucrose isomerase gene[J].Applied and Environmental Microbiology, 2005, 71(3):1581-1590.
[16] ZHANG D H, LI X Z, ZHANG L H.Isomaltulose synthase from Klebsiella sp.strain LX3 gene cloning and characterization and engineering of thermostability[J].Applied and Environmental Microbiology, 2002, 68(6):2676-2682.
[17] LIU J T, WU J, CHEN S.Expression and production optimization of sucrose isomerase from Pantoea dispersa in Escherichia coli[J].Chinese Journal of Biotechnology, 2016, 32(8):1070-1080.
[18] CHA J, JUNG J H, PARK S E, et al.Molecular cloning and functional characterization of a sucrose isomerase (isomaltulose synthase) gene from Enterobacter sp.FMB-1[J].Journal of Applied Microbiology, 2009, 107(4):1119-1130.
[19] DUAN X G, CHENG S, AI Y X, et al.Enhancing the thermostability of Serratia plymuthica sucrose isomerase using B-factor-directed mutagenesis[J].PLoS One, 2016, 11(2):e0149208.
[20] NAGAI Y, SUGITANI T, TSUYUKI K.Characterization of alpha-glucosyltransferase from Pseudomonas mesoacidophila MX-45[J].Bioscience, Biotechnology, and Biochemistry, 1994, 58(10):1789-1793.
[21] KAWAGUTI H Y, CELESTINO É M, MORAES A L L, et al.Characterization of a glucosyltransferase from Erwinia sp.D12 and the conversion of sucrose into isomaltulose by immobilized cells[J].Biochemical Engineering Journal, 2010, 48(2):211-217.
[22] 卢汉浪, 许黎明, 吕军, 等.亚硝基胍诱变选育高转化率异麦芽酮糖菌株[J].中国食品添加剂, 2012, 23(6):102-106.
LU H L, XU L M, LV J, et al.Screening of high isomaltulose-conversion rate Protaminobacter rubrum strain by NTG mutation[J].China Food Additives, 2012, 23(6):102-106.
[23] 张洪达. 高产异麦芽酮糖菌的诱变及性质研究[D].大连:大连工业大学, 2017.
ZHANG H D.Mutagenesis and properties of isomaltulose-producing bacteria[D].Dalian:Dalian Polytechnic University, 2017.
[24] 彭丹丹, 刘亚楠, 汪佳人, 等.蔗糖异构酶产生菌的常压室温等离子体诱变育种及发酵条件优化[J].河南工业大学学报(自然科学版), 2022, 43(2):63-69;78.
PENG D D, LIU Y N, WANG J R, et al.Atmospheric and room temperature plasma breeding and fermentation conditions optimization of sucrose isomerase producing strains[J].Journal of Henan University of Technology (Natural Science Edition), 2022, 43(2):63-69; 78.
[25] KIM Y, KOO B S, LEE H C, et al.Improved production of isomaltulose by a newly isolated mutant of Serratia sp.cells immobilized in calcium alginate[J].Canadian Journal of Microbiology, 2015, 61(3):193-199.
[26] 邓静, 吴华昌.不同诱变方法对米曲霉酶系的影响[J].中国酿造, 2005, 24(12):39-42.
DENG J, WU H C.Effect of different mutation methods on enzyme system of Aspergillus oryzame[J].China Brewing, 2005, 24(12):39-42.
[27] KAWAGUTI H Y, HARUMI SATO H.Effect of concentration and substrate flow rate on isomaltulose production from sucrose by Erwinia sp.cells immobilized in calcium-alginate using packed bed reactor[J].Applied Biochemistry and Biotechnology, 2010, 162(1):89-102.
[28] RAVAUD S, ROBERT X, WATZLAWICK H, et al.Insights into sucrose isomerization from crystal structures of the Pseudomonas mesoacidophila MX-45 sucrose isomerase, MutB[J].Biocatalysis and Biotransformation, 2008, 26(1-2):111-119.
[29] 马志宇, 高向红, 庞焦, 等.融合卷曲螺旋结构域的蔗糖异构酶活性包涵体异源表达及其酶学性质[J].中国生物制品学杂志, 2023, 36(7):793-799.
MA Z Y, GAO X H, PANG J, et al.Heterologous expression and enzymatic properties of active inclusion bodies of sucrose isomerase fused with coiled-coil domain[J].Chinese Journal of Biologicals, 2023, 36(7):793-799.
[30] PARK J Y, JUNG J H, SEO D H, et al.Microbial production of palatinose through extracellular expression of a sucrose isomerase from Enterobacter sp.FMB-1 in Lactococcus lactis MG1363[J].Bioresource Technology, 2010, 101(22):8828-8833.
[31] WU L T, WU S S, QIU J J, et al.Green synthesis of isomaltulose from cane molasses by Bacillus subtilis WB800-pHA01-PalI in a biologic membrane reactor[J].Food Chemistry, 2017, 229:761-768.
[32] ZHAN Y J, ZHU P, LIANG J F, et al.Economical production of isomaltulose from agricultural residues in a system with sucrose isomerase displayed on Bacillus subtilis spores[J].Bioprocess and Biosystems Engineering, 2020, 43(1):75-84.
[33] 程胜, 段绪果, 吴敬.重组蔗糖异构酶的制备及应用条件优化[J].食品与发酵工业, 2015, 41(5):41-47.
CHENG S, DUAN X G, WU J.Studies on the preparation of sucrose isomerase and its application for the production of isomaltulose[J].Food and Fermentation Industries, 2015, 41(5):41-47.
[34] 刘军彤. Pantoea dispersa蔗糖异构酶的重组表达及应用研究[D].无锡:江南大学, 2016.
LIU J T.Recombinant expression and application of Pantoea dispersa sucrose isomerase[D].Wuxi:Jiangnan University, 2016.
[35] ZHANG F, CHENG F, JIA D X, et al.Characterization of a recombinant sucrose isomerase and its application to enzymatic production of isomaltulose[J].Biotechnology Letters, 2021, 43(1):261-269.
[36] GUO D, LI M Y, JIANG M T, et al.Enhanced extracellular production and characterization of sucrose isomerase in Bacillus subtilis with optimized signal peptides[J].Foods, 2022, 11(16):2468.
[37] 宋蕾, 李宪臻, 郭小宇.蔗糖异构酶PalI在解脂耶氏酵母中的高水平表达及酶学性质表征[J].大连工业大学学报, 2022, 41(2):79-85.
SONG L, LI X Z, GUO X Y.High expression and characterization of sucrose isomerase PalI in Yarrowia lipolytica[J].Journal of Dalian Polytechnic University, 2022, 41(2):79-85.
[38] BACH C X, THI KIM ANH D, THANH THUY N, et al.Cloning of sucrose isomerase encoding gene from Klebsiella singaporensis ISB-36 and its expression in Pichia pastoris[J].Vietnam Journal of Biotechnology, 2020, 17(4):749-756.
[39] LI L J, WANG H W, CHENG H R, et al.Isomaltulose production by yeast surface display of sucrose isomerase from Pantoea dispersa on Yarrowia lipolytica[J].Journal of Functional Foods, 2017, 32:208-217.
[40] ZHANG P, WANG Z P, SHENG J, et al. High and efficient isomaltulose production using an engineered Yarrowia lipolytica strain[J]. Bioresource Technology, 2018, 265: 577-580.
[41] 邹亮. Pantoea dispersa蔗糖异构酶在芽孢杆菌中的表达及发酵优化[D]. 无锡: 江南大学, 2019.
ZOU, L. Expression and fermentation optimization of Pantoea dispersa sucrose isomerase in Bacillus subtilis[D]. Wuxi: Jiangnan University, 2019.
[42] TAI M, STEPHANOPOULOS G.Engineering the push and pull of lipid biosynthesis in oleaginous yeast Yarrowia lipolytica for biofuel production[J].Metabolic Engineering, 2013, 15:1-9.
[43] ZHANG P, WANG Z P, LIU S, et al.Overexpression of secreted sucrose isomerase in Yarrowia lipolytica and its application in isomaltulose production after immobilization[J].International Journal of Biological Macromolecules, 2019, 121:97-103.
[44] LI S, XU H, YU J G, et al.Enhancing isomaltulose production by recombinant Escherichia coli producing sucrose isomerase:Culture medium optimization containing agricultural wastes and cell immobilization[J].Bioprocess and Biosystems Engineering, 2013, 36(10):1395-1405.
[45] 宋蕾. 蔗糖异构酶的异源表达及其酶学性质表征[D].大连:大连工业大学, 2021.
SONG L.Heterologous expression of sucrose isomerase and characterization of its enzymatic properties[D].Dalian:Dalian Polytechnic University, 2021.
[46] SARDIÑA-PEÑA A J, MESA-RAMOS L, IGLESIAS-FIGUEROA B F, et al.Analyzing current trends and possible strategies to improve sucrose isomerases' thermostability[J].International Journal of Molecular Sciences, 2023, 24(19):14513.
[47] CHICA R A, DOUCET N, PELLETIER J N.Semi-rational approaches to engineering enzyme activity:Combining the benefits of directed evolution and rational design[J].Current Opinion in Biotechnology, 2005, 16(4):378-384.
[48] PILAK P, SCHIEFNER A, SEIBOTH J, et al.Engineering a highly active sucrose isomerase for enhanced product specificity by using a “battleship” strategy[J].ChemBioChem, 2020, 21(15):2161-2169.
[49] LIPSKI A, WATZLAWICK H, RAVAUD S, et al.Mutations inducing an active-site aperture in Rhizobium sp.sucrose isomerase confer hydrolytic activity[J].Acta Crystallographica Section D, 2013, 69(2):298-307.
[50] 程胜. Serratia plymuthica蔗糖异构酶的重组表达、热稳定性改造及应用研究[D]. 无锡: 江南大学, 2015.
CHENG S. Expression, thermostability modification and application of sucrose isomerase from Serratia plymuthica[D]. Wuxi: Jiangnan University,2015.
[51] SARDIÑA-PEÑA A J, BALLINAS-CASARRUBIAS L, SIQUEIROS-CENDÓN T S, et al.Thermostability improvement of sucrose isomerase PalI NX-5:A comprehensive strategy[J].Biotechnology Letters, 2023, 45(7):885-904.
[52] LIU H J, XING X Y, LU F P, et al.Functional Modification of the Substrate-Binding Site for Isomaltulose Production Based on Predicted Structure of Sucrose Isomerase from Pantoea dispersa UQ68 J[M].Lecture Notes in Electrical Engineering.Singapore:Springer Singapore, 2017:59-68.
[53] XU L J, KUAN S L, WEIL T.Contemporary approaches for site-selective dual functionalization of proteins[J].Angewandte Chemie International Edition, 2021, 60(25):13757-13777.
[54] SHAW B F, SCHNEIDER G F, BILGIÇER B, et al.Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation[J].Protein Science, 2008, 17(8):1446-1455.
[55] O'BRIEN A M, SMITH A T, Ó'FÁGÁIN C.Effects of phthalic anhydride modification on horseradish peroxidase stability and activity[J].Biotechnology and Bioengineering, 2003, 81(2):233-240.
[56] NAVAPOUR L, MOGHARRAB N.Structural insights into the effects of charge-reversal substitutions at the surface of horseradish peroxidase[J].Molecular Biology Research Communications, 2016, 5(3):175-192.
[57] LIU J Z, WANG M.Improvement of activity and stability of chloroperoxidase by chemical modification[J].BMC Biotechnology, 2007, 7:23.
[58] 熊亚红, 吴巧儿, 苏健鸿.化学修饰木瓜蛋白酶的酶学性质研究[J].分子催化, 2010, 24(6):529-536.
XIONG Y H, WU Q E, SU J H.Study on the enzymatic property of chemical modification papain[J].Journal of Molecular Catalysis, 2010, 24(6):529-536.
[59] MATSUMOTO M, NAKAGAWA T, UCHIDA Y, et al.Effect of modification of citraconic anhydrides on catalytic activity and thermostability of enzymes[J].Journal of Chemical Technology & Biotechnology, 2016, 91(1):59-64.
[60] LU M Y, GAO Z X, XING S Q, et al.Purification, characterization, and chemical modification of Bacillus velezensis SN-14 fibrinolytic enzyme[J].International Journal of Biological Macromolecules, 2021, 177:601-609.
[61] BAO C Y, ZHANG Q.Modulation of protein activity and assembled structure by polymer conjugation:PEGylation vs glycosylation[J].European Polymer Journal, 2019, 112:263-272.
[62] KISLEY L, MILLER K A, DAVIS C M, et al.Soluble zwitterionic poly (sulfobetaine) destabilizes proteins[J].Biomacromolecules, 2018, 19(9):3894-3901.
[63] ZHU G Y, WANG P.Polymer-enzyme conjugates can self-assemble at oil/water interfaces and effect interfacial biotransformations[J].Journal of the American Chemical Society, 2004, 126(36):11132-11133.
[64] WEINGÄRTNER H, CABRELE C, HERRMANN C.How ionic liquids can help to stabilize native proteins[J].Physical Chemistry Chemical Physics, 2012, 14(2):415-426.
[65] JIA R, HU Y, LIU L, et al.Enhancing catalytic performance of porcine pancreatic lipase by covalent modification using functional ionic liquids[J].ACS Catalysis, 2013, 3(9):1976-1983.
[66] LI X J, ZHANG C, LI S, et al.Improving catalytic performance of Candida rugosa lipase by chemical modification with polyethylene glycol functional ionic liquids[J].Industrial & Engineering Chemistry Research, 2015, 54(33):8072-8079.
[67] XU C, SUO H B, XUE Y, et al.Experimental and theoretical evidence of enhanced catalytic performance of lipase B from Candida Antarctica acquired by the chemical modification with amino acid ionic liquids[J].Molecular Catalysis, 2021, 501:111355.
[68] XU C, YIN X H, ZHANG C, et al.Improving catalytic performance of burkholderiacepacia lipase by chemical modification with functional ionic liquids[J].Chemical Research in Chinese Universities, 2018, 34(2):279-284.
[69] 张晓光, 裴新华, 伍慧兰, 等.疏水性脯氨酸离子液体化学修饰提升猪胰脂肪酶催化性能[J].高校化学工程学报, 2023, 37(2):268-275.
ZHANG X G, PEI X H, WU H L, et al.Improving catalytic performance of porcine pancreatic lipase by chemical modification using hydrophobic proline ionic liquid[J].Journal of Chemical Engineering of Chinese Universities, 2023, 37(2):268-275.
[70] SHANNON D A, WEERAPANA E.Covalent protein modification:The current landscape of residue-specific electrophiles[J].Current Opinion in Chemical Biology, 2015, 24:18-26.
[71] KRISHNAMURTHY A, MUNDRA S, BELUR P D.Improving the catalytic efficiency of fibrinolytic enzyme from Serratia marcescens subsp.sakuensis by chemical modification[J].Process Biochemistry, 2018, 72:79-85.
[72] GALVIS M, BARBOSA O, RUIZ M, et al.Chemical amination of lipase B from Candida Antarctica is an efficient solution for the preparation of crosslinked enzyme aggregates[J].Process Biochemistry, 2012, 47(12):2373-2378.
[73] CHOWDHURY R, STROMER B, POKHAREL B, et al.Control of enzyme-solid interactions via chemical modification[J].Langmuir, 2012, 28(32):11881-11889.
[74] TONG Y J, XIN Y, YANG H L, et al.Efficient improvement on stability of sarcosine oxidase via poly-lysine modification on enzyme surface[J].International Journal of Biological Macromolecules, 2014, 67:140-146.
[75] BROGAN A P S, SHARMA K P, PERRIMAN A W, et al.Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150 ℃[J].Nature Communications, 2014, 5:5058.
[76] BHATTI H N, RASHID M H, ASGHER M, et al.Chemical modification results in hyperactivation and thermostabilization of Fusarium solani glucoamylase[J].Canadian Journal of Microbiology, 2007, 53(2):177-185.
[77] DARBY J F, ATOBE M, FIRTH J D, et al.Increase of enzyme activity through specific covalent modification with fragments[J].Chemical Science, 2017, 8(11):7772-7779.
[78] GODOY C A, DE LAS RIVAS B, FILICE M, et al.Enhanced activity of an immobilized lipase promoted by site-directed chemical modification with polymers[J].Process Biochemistry, 2010, 45(4):534-541.
[79] ROMERO O, DE LAS RIVAS B, LOPEZ-TEJEDOR D, et al.Effect of site-specific peptide-tag labeling on the biocatalytic properties of thermoalkalophilic lipase from Geobacillus thermocatenulatus[J].ChemBioChem, 2018, 19(4):369-378.
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