Preparation and characterization of adsorption-crosslinking immobilized sucrose isomerase

  • CHEN Ning ,
  • CHANG Baogen ,
  • SHI Nian ,
  • LU Fuping ,
  • LIU Fufeng
Expand
  • (Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education;Tianjin Key Laboratory of Industrial Microbiology;National Engineering Laboratory for Industrial Enzymes;College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China)

Received date: 2022-03-11

  Revised date: 2021-03-21

  Online published: 2022-11-01

Abstract

Isomaltulose is a natural isomer of sucrose. It is widely used as a functional sweetener with promising properties, including slower digestion, prolonged energy release, lower insulin reaction, and less cariogenicity. The isomaltulose production by sucrose isomerase (SIase) isomerization catalyzing sucrose to produce isomaltulose is the most common method at present. SIase was immobilized on silica nanoparticle (SNP) cross-linked with glutaraldehyde (GA) by adsorption and adsorption-crosslinking method, and two immobilized enzyme, S-CLEAs and S-CLEAs-GA were obtained. The enzyme activity recovery of S-CLEAs reached up to 51.2% under the optimal condition of immobilization achieved with 6.25 mg/mL of SNP, 8.6 U/mL of SIase and 5 h of adsorption time. Then adding 0.08% GA and cross-linking 2 h, While the maximum activity recovery of S-CLEAs-GA was 44.9% when the GA concentration was 0.08% and cross-linking time was 2 h. Compared with free SIase, immobilized enzymes were maintained a relatively high enzyme activity in wide temperature and pH ranges. In addition, after 15 repeated uses, S-CLEAs-GA and S-CLEAs still had 55.1% and 77.9% of initial enzyme activity respectively. The above research results showed that immobilized SIase had excellent thermal, pH and operational stabilities, especially S-CLEAs-GA, thus had a good prospect of industrial application。

Cite this article

CHEN Ning , CHANG Baogen , SHI Nian , LU Fuping , LIU Fufeng . Preparation and characterization of adsorption-crosslinking immobilized sucrose isomerase[J]. Food and Fermentation Industries, 2022 , 48(19) : 9 -15 . DOI: 10.13995/j.cnki.11-1802/ts.031520

References

[1] 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):1 868-1 881.
[2] SAWALE P D, SHENDURSE A M, MOHAN M S, et al.Isomaltulose (palatinose):An emerging carbohydrate[J].Food Bioscience, 2017, 18:46-52.
[3] 张艳苓. 异麦芽酮糖的研究与应用[J].轻工科技, 2013, 29(5):23-24;59.
ZHANG Y L.Study and application of isomaltulose[J].Light Industry Science and Technology, 2013, 29(5):23-24;59.
[4] DE GROOT E, SCHWEITZER L, THEIS S.Efficacy of isomaltulose compared to sucrose in modulating endothelial function in overweight adults[J].Nutrients, 2020, 12(1):141.
[5] SHYAM S, RAMADAS A, CHANG S K.Isomaltulose:Recent evidence for health benefits[J].Journal of Functional Foods, 2018, 48:173-178.
[6] LINA B A R, JONKER D, KOZIANOWSKI G.Isomaltulose (Palatinose®):A review of biological and toxicological studies[J].Food and Chemical Toxicology, 2002, 40(10):1 375-1 381.
[7] CONTESINI F J, IBARGUREN C, GROSSO C R F, et al.Immobilization of glucosyltransferase from Erwinia sp.using two different techniques[J].Journal of Biotechnology, 2012, 158(3):137-143.
[8] WU L T, LIU Y, CHI B, et al.An innovative method for immobilizing sucrose isomerase on ε-poly-L-lysine modified mesoporous TiO2[J].Food Chemistry, 2015, 187:182-188.
[9] WU L T, QIU J J, WU S S, et al.Bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose[J].Advanced Synthesis & Catalysis, 2016, 358(24):4 030-4 040.
[10] 孟虹, 赵怡, 李宪臻, 等.蔗糖异构酶PalⅠ-Cu2+纳米花固定化酶的制备及其结构、性能分析[J].中国生物制品学杂志, 2021, 34(3):286-289;293.
MENG H, ZHAO Y, LI X Z, et al.Preparation, structure and performance of sucrose isomerase PalⅠ-Cu2+ nanoflower as an immobilized enzyme[J].Chinese Journal of Biologicals, 2021, 34(3):286-289;293.
[11] ZHANG C Y, DONG X Y, GUO Z, et al.Remarkably enhanced activity and substrate affinity of lipase covalently bonded on zwitterionic polymer-grafted silica nanoparticles[J].Journal of Colloid and Interface Science, 2018, 519:145-153.
[12] PERWEZ M, AHMED MAZUMDER J, SARDAR M.Preparation and characterization of reusable magnetic combi-CLEA of cellulase and hemicellulase[J].Enzyme and Microbial Technology, 2019, 131:109389.
[13] SIGURDARDÓTTIR S B, LEHMANN J, OVTAR S, et al.Enzyme immobilization on inorganic surfaces for membrane reactor applications:Mass transfer challenges, enzyme leakage and reuse of materials[J].Advanced Synthesis & Catalysis, 2018, 360(14):2 578-2 607.
[14] ALI S, ZAFAR W, SHAFIQ S, et al.Enzymes immobilization:An overview of techniques, support materials and its applications[J].International Journal of Scientific & Technology Research, 2017, 6(7):64-72.
[15] 叶芊芊, 谌凯, 张玲, 等.京尼平交联制备枯草杆菌碱性蛋白酶聚集体[J].现代食品科技, 2020, 36(8):95-101;152.
YE Q Q, CHEN K, ZHANG L, et al.Preparation of Bacillus subtilis alkaline protease aggregates by crosslinking with genepin[J].Modern Food Science and Technology, 2020, 36(8):95-101;152.
[16] 许超群, 万云宝, 张小龙, 等.吸附交联法固定化黑曲霉β-葡萄糖苷酶[J].中国酿造, 2016, 35(4):83-87.
XU C Q, WAN Y B, ZHANG X L, et al.Immobilization of β-glucosidase from Aspergillus niger by adsorption and crosslinking method[J].China Brewing, 2016, 35(4):83-87.
[17] YANG X Y, CHEN Y F, YAO S, et al.Preparation of immobilized lipase on magnetic nanoparticles dialdehyde starch[J].Carbohydrate Polymers, 2019, 218:324-332.
[18] NAWAWI N N, HASHIM Z, MANAS N H A, et al.A porous-cross linked enzyme aggregates of maltogenic amylase from Bacillus lehensis G1:Robust biocatalyst with improved stability and substrate diffusion[J].International Journal of Biological Macromolecules, 2020, 148:1 222-1 231.
[19] YE P, JIANG J, XU Z K.Adsorption and activity of lipase from Candida rugosa on the chitosan-modified poly(acrylonitrile-co-maleic acid) membrane surface[J].Colloids and Surfaces B:Biointerfaces, 2007, 60(1):62-67.
[20] FILHO D G, SILVA A G, GUIDINI C Z.Lipases:sources, immobilization methods, and industrial applications[J].Applied Microbiology and Biotechnology, 2019, 103(18):7 399-7 423.
[21] ESMAEILNEJAD-AHRANJANI P, KAZEMEINI M, SINGH G, et al.Study of molecular conformation and activity-related properties of lipase immobilized onto core-shell structured polyacrylic acid-coated magnetic silica nanocomposite particles[J].Langmuir:the ACS Journal of Surfaces and Colloids, 2016, 32(13):3 242-3 252.
[22] URRUTIA P, ARRIETA R, ALVAREZ L, et al.Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil:The impact of support functionalization on lipase activity, selectivity and stability[J].International Journal of Biological Macromolecules, 2018, 108:674-686.
[23] CHEN N, ZHANG C Y, DONG X Y, et al.Fabrication and characterization of epoxylated zwitterionic copolymer-grafted silica nanoparticle as a new support for lipase immobilization[J].Chinese Journal of Chemical Engineering, 2020, 28(4):1 129-1 135.
[24] ZHANG C Y, LIU Y, SUN Y.Lipase immobilized to a short alkyl chain-containing zwitterionic polymer grafted on silica nanoparticles:Moderate activation and significant increase of thermal stability[J].Biochemical Engineering Journal, 2019, 146:124-131.
[25] TUMTURK H, YÜKSEKDAG H.Acetylcholinesterase immobilized onto PEI-coated silica nanoparticles[J].Artificial Cells, Nanomedicine, and Biotechnology, 2016, 44(2):443-447.
[26] NGUYEN L N, HAI F I, DOSSETO A, et al.Continuous adsorption and biotransformation of micropollutants by granular activated carbon-bound laccase in a packed-bed enzyme reactor[J].Bioresource Technology, 2016, 210:108-116.
[27] 陈宁, 延文星, 路福平, 等.磷脂酶D交联聚集体的制备及其酶学性能研究[J].食品与发酵工业, 2022, 48(5):1-7.
CHEN N, YAN W X, LU F P, et al.Preparation and characterization of cross-linked enzyme aggregates of phospholipase D[J].Food and Fermentation Industries, 2022, 48(5):1-7.
Outlines

/