Characterization of Cross-Linked Enzyme Aggregates (CLEAs) of Tyrosinase from Volvariella volvacea
Abstract
Mushroom is considered as a cheap source of tyrosinase for L-3,4-dihydroxyphenylalanine (L-DOPA) production. Tyrosinase extracted from fresh straw mushroom (Volvariella volvacea) was concentrated by ammonium sulfate precipitation and immobilized as cross-linked enzyme aggregates (CLEAs) with the optimal glutaraldehyde concentration of 1.5% (v/v) at 4 oC for 16 h. The optimum pH and temperature on CLEAs-tyrosinase activity was found at 7.0 and 40 oC, respectively while the free tyrosinase exhibited pH and temperature optima at 6.0 and 30 oC, respectively. The apparent Km and Vmax values of CLEAs-tyrosinase for L-tyrosine were 0.261±0.057 mM and 0.053±0.0081 mM min-1, respectively. The CLEAs tyrosinase retained 50% activity after three reuses with 4 h of each reaction cycle. The CLEAs tyrosinase with the specific activity of 12.3 units/g could produce 0.0025 mM L-DOPA in 2 h under the optimized conditions. Keywords: enzyme immobilization, cross linked enzyme aggregates, tyrosinase, Volvariella volvaceaReferences
Arica MY., Senel S., Alaeddinoglu NG., Patir S. and Denizli A. 2000. Invertase immobilized on spacer-arm attached poly (hydroxyethyl methacrylate) membrane: preparation and properties. Journal of Applied Polymer Science, 75, 1685–1692.
Arnow L. 1937. Colorimetric determination of the components of 3,4-dihydroxyphenylalanine-tyrosine mixtures. Journal of Biological Chemistry, 118, 531–537.
Araya E., Urrutia P., Romero O., Illanes A., and Wilson L. 2019. Design of combined cross linked enzyme aggregates (combi-CLEAs) of β-galactosidase and glucose isomerase for the one-pot production of fructose syrup from lactose. Food Chemistry, 288, 102–107.
Aytar BS. and Bakir U. 2008. Preparation of cross-linked tyrosinase aggregation. Process Biochemistry, 43,
125-131.
Cerdobble A., Winter KDc. and Desmet T. 2010. Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial application. Biotechnology Journal, 5, 1192-1197.
Dong T., Zhao L., Huang Y., and Tan X. 2010. Preparation of cross-linked aggregates of aminoacylase from Aspergillus mellueus by using bovine serum albumin as an inert additive. Bioresource Technology,
101, 6569-6571.
Lowry OH., Rosenbrough NJ., Farr A., and Randall RJ. 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265-275.
Migneault I., Dartiguenave C., and Bertrand M.J. 2004. Glutaraldehyde: behavior in aqueous solution, reaction with proteins and application to enzyme cross-linking. Biotechniques, 37, 790-802.
Mahmod SS., Yusof F., Jami MS., and Khanahmadi S. 2016. Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease. Bioresources and Bioprocessing, 3, 1-11.
Nagutsu T and Sawada M. 2009. L-DOPA therapy for Parkinson’s disease: past, present, and future, Parkinsonnism and Related Disorders, 15, S3-S8.
Robb DA. 1984. Copper Protein and Copper Enzymes. Vol II. Boca Raton. CRC Press. p. 207-241.
Seo SY., Sharma VK., and Sharma N. 2003. Mushroom tyrosinase: recent prospects. Journal of Agricultural and Food Chemistry, 52, 2837-2853.
Sheldon RA. 2007. Cross-linked enzyme aggregates: stable and recyclable biocatalysts. Biochemical Society Transactions, 35, 1583-1587.
Sheldon RA. 2011. Cross-linked enzyme aggregates as industrial biocatalysts. Organic Process Research and Development, 15, 213-223.
Sheldon RA., and VanPelt. S. 2013. Enzyme immobilization in biocatalysis: Why, what and how. Chemical Society Reviews, 42(15), 6223-6235.
Xu DY., Chen JY., and Yang Z. 2012. Use of cross-linked tyrosinase aggregates as catalyst for synthesis of L-DOPA. Biochemical Engineering Journal, 63, 88-94.
Yu C., Li X., Lou W., and Zong M. 2013. Cross-linked enzyme aggregates of Mung bean epoxide hydrolases: A highly active, stable and recyclable biocatalysts for asymmetric hydrolysis of epoxides. Journal of Biotechnology, 166, 12-19.
Arnow L. 1937. Colorimetric determination of the components of 3,4-dihydroxyphenylalanine-tyrosine mixtures. Journal of Biological Chemistry, 118, 531–537.
Araya E., Urrutia P., Romero O., Illanes A., and Wilson L. 2019. Design of combined cross linked enzyme aggregates (combi-CLEAs) of β-galactosidase and glucose isomerase for the one-pot production of fructose syrup from lactose. Food Chemistry, 288, 102–107.
Aytar BS. and Bakir U. 2008. Preparation of cross-linked tyrosinase aggregation. Process Biochemistry, 43,
125-131.
Cerdobble A., Winter KDc. and Desmet T. 2010. Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial application. Biotechnology Journal, 5, 1192-1197.
Dong T., Zhao L., Huang Y., and Tan X. 2010. Preparation of cross-linked aggregates of aminoacylase from Aspergillus mellueus by using bovine serum albumin as an inert additive. Bioresource Technology,
101, 6569-6571.
Lowry OH., Rosenbrough NJ., Farr A., and Randall RJ. 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265-275.
Migneault I., Dartiguenave C., and Bertrand M.J. 2004. Glutaraldehyde: behavior in aqueous solution, reaction with proteins and application to enzyme cross-linking. Biotechniques, 37, 790-802.
Mahmod SS., Yusof F., Jami MS., and Khanahmadi S. 2016. Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease. Bioresources and Bioprocessing, 3, 1-11.
Nagutsu T and Sawada M. 2009. L-DOPA therapy for Parkinson’s disease: past, present, and future, Parkinsonnism and Related Disorders, 15, S3-S8.
Robb DA. 1984. Copper Protein and Copper Enzymes. Vol II. Boca Raton. CRC Press. p. 207-241.
Seo SY., Sharma VK., and Sharma N. 2003. Mushroom tyrosinase: recent prospects. Journal of Agricultural and Food Chemistry, 52, 2837-2853.
Sheldon RA. 2007. Cross-linked enzyme aggregates: stable and recyclable biocatalysts. Biochemical Society Transactions, 35, 1583-1587.
Sheldon RA. 2011. Cross-linked enzyme aggregates as industrial biocatalysts. Organic Process Research and Development, 15, 213-223.
Sheldon RA., and VanPelt. S. 2013. Enzyme immobilization in biocatalysis: Why, what and how. Chemical Society Reviews, 42(15), 6223-6235.
Xu DY., Chen JY., and Yang Z. 2012. Use of cross-linked tyrosinase aggregates as catalyst for synthesis of L-DOPA. Biochemical Engineering Journal, 63, 88-94.
Yu C., Li X., Lou W., and Zong M. 2013. Cross-linked enzyme aggregates of Mung bean epoxide hydrolases: A highly active, stable and recyclable biocatalysts for asymmetric hydrolysis of epoxides. Journal of Biotechnology, 166, 12-19.
Downloads
Published
2019-09-25
Issue
Section
บทความวิจัยจากการประชุมวิชาการระดับชาติ"วิทยาศาสตร์วิจัย"ครั้งที่ 11
