The purified and thermo stable myrosinase from cauliflower seedlings was immobilized by 3.5% agar agar matrix and immobilized myrosinase chips were stored in extraction buffer. After 48 hours 30% enzyme activity was exuded into extraction media from immobilized enzyme chips. Effect of some metal ions and organic solvents on the activity of immobilized cauliflower myrosinase was studied. Amongst selective metal ions (Sr2+, Sn2+ and Ba2+), Sr2+ at 4 mM concentration exhibited marked activating effect on the activity up to 3 fold. However, Sn2+ and Ba2+ increased the activity to a certain extent and then suppressed. Activation kinetics of myrosinase in presence of Sn2+ and Sr2+ were studied between 0-20min.The rate of reaction was almost constant till 15 min and then slight deactivation was recorded at various concentrations used. On the other hand, few heavy metal ions [Fe2+, Fe3+, Cu2+ and Zn2+] strongly inhibited the activity even at lower concentrations. Several nonpolar organic solvents even at comparatively higher concentrations had detectable activation effects. Further, their activity was seen with respect totime (27 min). However, some protic polar organic solvents exhibited inhibitory effect with immobilized myrosinase except to butanol.
| Published in | Advances in Biochemistry (Volume 1, Issue 3) |
| DOI | 10.11648/j.ab.20130103.12 |
| Page(s) | 51-56 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2013. Published by Science Publishing Group |
Myrosinase, Cauliflower, Immobilization, Agar Agar, Metal Ions, Organic Solvent
| [1] | M.F. Chaplin, and C.Bucke, The large scale use of enzymes in solution. Enzyme Technology, Cambridge University Press, 1990. |
| [2] | R.A.Sheldon, Enzyme Immobilization: the quest for optimum performance. Advanced Synthesis and Catalysis, 349: 1289-1307, 2007. |
| [3] | B.Krajewska, Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enzyme and Microbial Technol., 35: 126-139, 2004. |
| [4] | L.Q.Cao, Immobilised enzymes: science or art? Current Opinion in Chemical Biol., 9: 217-226,2005. |
| [5] | R.Iori,O.Leoni, and S.Palmieri, Immobilization of myrosinase (Thioglucoside glucohydrolase EC 3.2.3.1) Biotechnology Letters Vol10, 8, 575-578.1988. |
| [6] | O. Leoni,R.Iori, and S.Palmieri, Immobilization of myrosinase on membrane for determining the glucosinolate content of cruciferous material. J. Agric. Food Chem. 39, 2322−2326.1991 |
| [7] | O.Leoni, F.Felluga, and S.Palmieri, The formation of 2-hydroxybut-3-enyl cyanide from (2S)-2-hydroxybut-3-enyl glucosinolate using immobilized myrosinase. Tetrahedron Lett.49, 7967−7970.1993. |
| [8] | O.Leoni, CMarot,P. Rollin, SPalmieri, Preparation of (5R)-5-vinyloxazolidine-2-thione from natural epi-progoitrin using immobilized myrosinase. Tetrahedron Asymm.,5, 1157−1160,1994. |
| [9] | O.Leoni, R.Ioriand S.Palmieri, Hydrolysis of Glucosinolates Using Nylon-immobilized myrosinase to Produce Pure Bioactive Molecules. Biotechnology and Bioengineering.68 (6), 660-664, 2000. |
| [10] | M, M,F.Choi, M.M.K Liang and A W.M Lee, biosensing method with enzyme-immobilized eggshell membranes for determination of total glucosinolates in vegetables. Enzyme and Microbial Technology 36, 91–99.2005. |
| [11] | J.Cheng,S.M. Yu, and P.Zuo, Horseradish peroxidase immobilized on aluminium-pillared interlayered clay for the catalytic oxidation of phenolic wastewater. Water Res., 40, 283-290, 2006. |
| [12] | Y.Kulshrestha, andQ. Husain, Direct immobilization of peroxidase on DEAE cellulose from ammonium sulphate fractionated proteins of bitter gourd (Momordicacharantia). Enzyme Microb.Technol., 38, 470-477, 2006. |
| [13] | T.Romaskevic, SBudriene, K.Pielichowski and J.Pielichowski, Application of polyurethane-based materials for immobilization of enzymes and cells: A review. Chemija, 17, 74-89,2006. |
| [14] | K.N. Niladevi, and P.Prema, Immobilization of laccase from Streptomyces psammoticus and its application in phenol removal using packed bed reactor. World. J. Microbiol. Biotechnol.,24, 1215-1222,2008. |
| [15] | W.Tischer, and V.Kasche, Immobilized enzymes: Crystals or carriers. TIBTECH, 17, 326-335,1999. |
| [16] | Matto, M. and Husain, Q. (2006) Entrapment of porous and stable concanavalin A-peroxidase complex into hybrid calcium alginate-pectin gel. J. Chem. Technol. Biotechnol., 8, 1316-1323. |
| [17] | Palmieri, S., Leoni, O.andIori, R. (1982)A study- state study of myrosinase with direct ultraviolet spectrophotometric assay. Anal.Biochem.123, 320-324. |
| [18] | Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, P.J. (1951) Protein measurement with folin protein reagent. J. Biol. Chem., 193, 265–275. |
| [19] | Prakash,O. and Jaiswal,N.(2011)Immobilization of a Thermostable -Amylase on Agaroseand Agar Matrices and its Application in Starch Stain Removal, World Applied Sciences Journal 13,3, 572-577. |
| [20] | Tani, N., Ohtsuru, M. and Hata, T. (1974) Isolation of myrosinase producing microorganism. Agr. Biol. Chem. 38, 1617-1622. |
| [21] | Prakash, O., Rai,A K., Singh, J. and SinghP.M. (2013) Effect of Heavy Metal Ions and Carbohydrates on the Activityof Cauliflower (Brassica oleracea Var. botrytis) Myrosinase, journal of stress physiology & biochemistry Vol. 9 No. 2 pp.107-117. |
| [22] | Shafiei, M., Ziaee, A.A. and Amoozegar, M.A. (2011)Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J. Ind. Microbiol. Biotechnol.,38, 275–281. |
| [23] | Jaiswal,N. (2011) Physico chemical characterization and molecular studies of α-amylase from soybean seed.BHU, Varanasi. |
| [24] | Botti, G.M., Malcom, G.T. and Nigel, P. Botting. (1995) Studies on the mechanism of myrosinase, The journal of Biological chemistry. Vol. 270, No. 35, 20530- 20535. |
APA Style
Ajeet Kumar Rai, Om Prakash, Jagdish Singh, Prabhakar Mohan Singh. (2013). Immobilization of Cauliflower Myrosinase on Agar Agar Matrix and its Application with Various Effectors. Advances in Biochemistry, 1(3), 51-56. https://doi.org/10.11648/j.ab.20130103.12
ACS Style
Ajeet Kumar Rai; Om Prakash; Jagdish Singh; Prabhakar Mohan Singh. Immobilization of Cauliflower Myrosinase on Agar Agar Matrix and its Application with Various Effectors. Adv. Biochem. 2013, 1(3), 51-56. doi: 10.11648/j.ab.20130103.12
AMA Style
Ajeet Kumar Rai, Om Prakash, Jagdish Singh, Prabhakar Mohan Singh. Immobilization of Cauliflower Myrosinase on Agar Agar Matrix and its Application with Various Effectors. Adv Biochem. 2013;1(3):51-56. doi: 10.11648/j.ab.20130103.12
Share This Article
Twitter
Linked In
Facebook
Copy
Download@article{10.11648/j.ab.20130103.12,
author = {Ajeet Kumar Rai and Om Prakash and Jagdish Singh and Prabhakar Mohan Singh},
title = {Immobilization of Cauliflower Myrosinase on Agar Agar Matrix and its Application with Various Effectors},
journal = {Advances in Biochemistry},
volume = {1},
number = {3},
pages = {51-56},
doi = {10.11648/j.ab.20130103.12},
url = {https://doi.org/10.11648/j.ab.20130103.12},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20130103.12},
abstract = {The purified and thermo stable myrosinase from cauliflower seedlings was immobilized by 3.5% agar agar matrix and immobilized myrosinase chips were stored in extraction buffer. After 48 hours 30% enzyme activity was exuded into extraction media from immobilized enzyme chips. Effect of some metal ions and organic solvents on the activity of immobilized cauliflower myrosinase was studied. Amongst selective metal ions (Sr2+, Sn2+ and Ba2+), Sr2+ at 4 mM concentration exhibited marked activating effect on the activity up to 3 fold. However, Sn2+ and Ba2+ increased the activity to a certain extent and then suppressed. Activation kinetics of myrosinase in presence of Sn2+ and Sr2+ were studied between 0-20min.The rate of reaction was almost constant till 15 min and then slight deactivation was recorded at various concentrations used. On the other hand, few heavy metal ions [Fe2+, Fe3+, Cu2+ and Zn2+] strongly inhibited the activity even at lower concentrations. Several nonpolar organic solvents even at comparatively higher concentrations had detectable activation effects. Further, their activity was seen with respect totime (27 min). However, some protic polar organic solvents exhibited inhibitory effect with immobilized myrosinase except to butanol.},
year = {2013}
}
TY - JOUR T1 - Immobilization of Cauliflower Myrosinase on Agar Agar Matrix and its Application with Various Effectors AU - Ajeet Kumar Rai AU - Om Prakash AU - Jagdish Singh AU - Prabhakar Mohan Singh Y1 - 2013/08/30 PY - 2013 N1 - https://doi.org/10.11648/j.ab.20130103.12 DO - 10.11648/j.ab.20130103.12 T2 - Advances in Biochemistry JF - Advances in Biochemistry JO - Advances in Biochemistry SP - 51 EP - 56 PB - Science Publishing Group SN - 2329-0862 UR - https://doi.org/10.11648/j.ab.20130103.12 AB - The purified and thermo stable myrosinase from cauliflower seedlings was immobilized by 3.5% agar agar matrix and immobilized myrosinase chips were stored in extraction buffer. After 48 hours 30% enzyme activity was exuded into extraction media from immobilized enzyme chips. Effect of some metal ions and organic solvents on the activity of immobilized cauliflower myrosinase was studied. Amongst selective metal ions (Sr2+, Sn2+ and Ba2+), Sr2+ at 4 mM concentration exhibited marked activating effect on the activity up to 3 fold. However, Sn2+ and Ba2+ increased the activity to a certain extent and then suppressed. Activation kinetics of myrosinase in presence of Sn2+ and Sr2+ were studied between 0-20min.The rate of reaction was almost constant till 15 min and then slight deactivation was recorded at various concentrations used. On the other hand, few heavy metal ions [Fe2+, Fe3+, Cu2+ and Zn2+] strongly inhibited the activity even at lower concentrations. Several nonpolar organic solvents even at comparatively higher concentrations had detectable activation effects. Further, their activity was seen with respect totime (27 min). However, some protic polar organic solvents exhibited inhibitory effect with immobilized myrosinase except to butanol. VL - 1 IS - 3 ER -
Information
Email: