Abstract
Tyrosol β-galactoside (TG) is a phenylethanoid glycoside with proven neuroprotective properties. This work deals with its biocatalytic production from tyrosol and lactose using Aspergillus oryzae β-galactosidase in immobilized form. Six commercial carriers were examined to find the optimal biocatalyst. Besides standard biocatalyst performance characteristics, adsorption of the hydrophobic substrate on immobilization carrier matrices was also investigated. The adsorption of tyrosol was significant, but it did not have adverse effects on TG production. On the contrary, TG yield was improved for some biocatalysts. A biocatalyst prepared by covalent binding of β-galactosidase on an epoxy-activated carrier was used for detailed investigation of the effect of reaction conditions on glycoside production. Temperature had a surprisingly weak effect on the overall process rate. A lactose concentration of 0.83 M was found to be optimal to enhance TG formation. The impact of tyrosol concentration was rather complex. This substrate caused inhibition of all reactions. Its concentration had a strong effect on the hydrolysis of lactose and all products. Higher tyrosol concentrations, 30–40 g/L, were favorable as pseudo-equilibrium concentrations of TG and galactooligosaccharide were reached. Repeated batch results revealed excellent operational stability of the biocatalyst.
Similar content being viewed by others
Abbreviations
- TG:
-
Tyrosol β-galactoside
- GOS:
-
Galactooligosaccharides
- T:
-
Tyrosol
- Lac:
-
Lactose
- Glu:
-
Glucose
- Gal:
-
Galactose
- PS:
-
Polystyrene
- PS–DVB:
-
Polystyrene–divinylbenzene
References
Anter J, Tasset I, Demyda-Peyras S, Ranchal I, Moreno-Millan M, Romero-Jimenez M, Muntane J, Luque de Castro MD, Munoz-Serrano A, Alonso-Moraga A (2014) Mutat Res Genet Toxicol Environ Mutagen 772:25–33
Visioli F, Poli A, Gall C (2002) Med Res Rev 22:65–75
Waterman E, Lockwood B (2007) Altern Med Rev 12:331–342
De La Cruz JP, Ruiz-Moreno MI, Guerrero A, Reyes JJ, Benitez-Guerrero A, Espartero JL, Gonzalez-Correa JA (2015) J Agric Food Chem 63:5957–5963
Richard N, Arnold S, Hoeller U, Kilpert C, Wertz K, Schwager J (2011) Planta Med 77:1890–1897
Wani TA, Masoodi FA, Gani A, Baba WN, Rahmanian N, Akhter R, Wani IA, Ahmad M (2018) Trends Food Sci Technol 77:77–90
Mateos R, Trujillo M, Pereira-Caro G, Madrona A, Cert A, Espartero JL (2008) J Agric Food Chem 56:10960–10966
Atochin DN, Chernysheva GA, Smolyakova VI, Osipenko AN, Logvinov SV, Zhdankina AA, Sysolyatin SV, Kryukov YA, Anfinogenova Y, Plotnikova TM, Plotnikov MB (2016) Phytomedicine 23:784–792
Khodanovich MY, Kisel AA, Chernysheva GA, Smol'yakova VI, Kudabaeva MS, Krutenkova EP, Tyumentseva Ycapital AC, Plotnikov MB (2019) Bull Exp Biol Med 168:224–228
Omar SH, Kerr PG, Scott CJ, Hamlin AS, Obied HK (2017) Molecules 22:1858–1878
St-Laurent-Thibault C, Arseneault M, Longpré F, Ramassamy C (2011) Curr Alzheimer Res 8:543–551
de la Torre R (2008) Inflammopharmacology 16:245–247
Lee DH, Kim YJ, Kim MJ, Ahn J, Ha TY, Lee SH, Jang YJ, Jung CH (2016) Molecules 21:E128
Rodriguez-Morato J, Boronat A, Kotronoulas A, Pujadas M, Pastor A, Olesti E, Perez-Mana C, Khymenets O, Fito M, Farre M, de la Torre R (2016) Drug Metab Rev 48:218–236
Kang J, Kim YM, Kim N, Kim DW, Nam SH, Kim D (2009) Appl Microbiol Biotechnol 83:1009–1016
Prodanović R, Milosavić N, Sladić D, Zlatović M, Božić B, Ćirković Veličković T, Vujčić Z (2005) J Mol Catal B Enzym 35:142–146
Torres P, Poveda A, Jimenez-Barbero J, Parra JL, Comelles F, Ballesteros AO, Plou FJ (2011) Adv Synth Catal 353:1077–1086
Palmeri A, Mammana L, Tropea MR, Gulisano W, Puzzo D (2016) J Alzheimers Dis 52:65–75
Yu K, Zhao X, Wu W, Hong Z (2013) Tetrahedron Lett 54:2788–2790
Shi T, Chen H, Jing L, Liu X, Sun X, Jiang R (2011) Synth Commun 41:2594–2600
Herrera-Gonzalez A, Nunez-Lopez G, Morel S, Amaya-Delgado L, Sandoval G, Gschaedler A, Remaud-Simeon M, Arrizon J (2017) Appl Microbiol Biotechnol 101:5223–5234
Potocká E, Mastihubová M, Mastihuba V (2015) J Mol Catal B Enzym 113:23–28
Yang XP, Wang FF, Yan J, Ma K, Mao DB (2017) Biotechnol Appl Biochem 64:525–531
Yu HL, Xu JH, Lu WY, Lin GQ (2008) J Biotechnol 133:469–477
Bassanini I, Krejzova J, Panzeri W, Monti D, Kren V, Riva S (2017) Chemsuschem 10:2040–2045
Hollá V, Antošová M, Karkeszová K, Mastihuba V, Polakovič M (2019) Biotechnol J 14:e1800571
Karnišová Potocká E, Mastihubová M, Mastihuba V (2019) Biocatal Biotransform 37:18–24
Qi T, Gu G, Xu L, Xiao M, Lu L (2017) Appl Microbiol Biotechnol 101:4995–5003
Shi TY, Feng SF, Xing JH, Wu YM, Li XQ, Zhang N, Tian Z, Liu SB, Zhao MG (2012) Neurotox Res 21:358–367
Deng Y, Wang Q, Liu X, Wang Y, Ding Z (2011) Arzneimittelforschung 61:435–438
Nam SH, Park J, Jun W, Kim D, Ko JA, Abd El-Aty AM, Choi JY, Kim DI, Yang KY (2017) AMB Express 7:224
Nieto-Dominguez M, de Eugenio LI, Penalver P, Belmonte-Reche E, Morales JC, Poveda A, Jimenez-Barbero J, Prieto A, Plou FJ, Martinez MJ (2017) J Agric Food Chem 65:10526–10533
Nunez-Lopez G, Herrera-Gonzalez A, Hernandez L, Amaya-Delgado L, Sandoval G, Gschaedler A, Arrizon J, Remaud-Simeon M, Morel S (2019) Enzyme Microb Technol 122:19–25
Adamíková J, Antošová M, Polakovič M (2019) Biotechnol J 14:e1800120
Polakovič M, Švitel J, Bučko M, Filip J, Neděla V, Ansorge-Schumacher MB, Gemeiner P (2017) Biotechnol Lett 39:667–683
Zor T, Selinger Z (1996) Anal Biochem 236:302–308
Šimko I, Roriz E, Gramblička M, Illeová V, Polakovič M (2015) Food Bioprod Process 95:254–263
Ghazi I, De Segura AG, Fernández-Arrojo L, Alcalde M, Yates M, Rojas-Cervantes ML, Plou FJ, Ballesteros A (2005) J Mol Catal B Enzym 35:19–27
Sheldon RA, van Pelt S (2013) Chem Soc Rev 42:6223–6235
Tanriseven A, Aslan Y (2005) Enzyme Microb Technol 36:550–554
Acknowledgements
This work was supported by Grants from the Agency of the Ministry of Education, Science, Research and Sport of the Slovak Republic for Structural Funds of EU (Grant number: ITMS 26240220084), Slovak Research and Development Agency (Grant number: APVV-18-0188), and the Slovak Grant Agency for Science (Grant number: VEGA 1/0573/17). Ms. Alessandra Basso from Purolite company is acknowledged for kindly providing their carriers. Dr. Vladimír Mastihuba is kindly acknowledged for providing the tyrosol-β-d-galactoside standard.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare no conflict of interest.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Electronic supplementary material
Below is the link to the electronic supplementary material.
Rights and permissions
About this article
Cite this article
Hollá, V., Hill, R., Antošová, M. et al. Design of immobilized biocatalyst and optimal conditions for tyrosol β-galactoside production. Bioprocess Biosyst Eng 44, 93–101 (2021). https://doi.org/10.1007/s00449-020-02425-2
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00449-020-02425-2