dc.contributor.author |
Le Roes-Hill, Marilize
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|
dc.contributor.author |
Palmer, Zaida
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|
dc.contributor.author |
Rohland, Jeffrey
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|
dc.contributor.author |
Kirby, Bronwyn M.
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dc.contributor.author |
Burton, Stephanie G.
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dc.date.accessioned |
2015-12-03T09:02:54Z |
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dc.date.issued |
2015-12 |
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dc.description.abstract |
Actinomycetes are a ubiquitous group of bacteria, and are hypothesised to produce tyrosinases for pro-tection against the potential toxic effect of phenolic compounds and for the production of melanin. In thisstudy, tyrosinase production by Streptomyces pharetrae CZA14T(CZA14Tyr) and Streptomyces polyantibi-oticus SPRT(SPRTyr) was optimised. The enzymes were partially purified and biochemically characterisedto determine their suitability for industrial applications. SPRTyr was stable up to 40◦C and at pH 4.5–10.0,while CZA14Tyr was stable up to 40◦C and at pH 6.5–10.0. The enzymes showed variable stability in thepresence of water-miscible organic solvents and were able to oxidize l-DOPA in the presence of these sol-vents. A limited inhibitory effect was observed with arbutin, EDTA, sodium chloride and sodium dodecylsulphate, while both enzymes were strongly inhibited by the reducing agents used in this study. Inhibi-tion of enzyme activity was observed in the presence of 1 mM Cu2+and 5 mM Co2+for SPRTyr, and 5 mMFe2+and 5 mM Zn2+for CZA14Tyr. When applied in various cross-linking reactions both tyrosinases wereable to cross-link casein and gelatine in the absence of a phenolic compound, showing potential forapplication in the food industry and for the production of biomaterials. |
en_ZA |
dc.description.embargo |
2016-12-31 |
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dc.description.librarian |
hb2015 |
en_ZA |
dc.description.sponsorship |
National Research Foundation (NRF) of South Africa for project funding [Grant No. 73691] and Cape Peninsula University of Technology (CPUT) University Research Funding. |
en_ZA |
dc.description.uri |
http://www.elsevier.com/locate/molcatb |
en_ZA |
dc.identifier.citation |
Le Roes-Hill, M, Palmer, Z, Rohland, J, Kirby, BM & Burton, SG 2015, 'Partial purification and characterisation of two actinomycete tyrosinases and their application in cross-linking reactions', Journal of Molecular Catalysis B : Enzymatic, vol. 122, pp. 353-364. |
en_ZA |
dc.identifier.issn |
1381-1177 (print) |
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dc.identifier.issn |
1873-3158 (online) |
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dc.identifier.other |
10.1016/j.molcatb.2015.10.012 |
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dc.identifier.uri |
http://hdl.handle.net/2263/51040 |
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dc.language.iso |
en |
en_ZA |
dc.publisher |
Elsevier |
en_ZA |
dc.rights |
© 2015 Elsevier B.V. All rights reserved. Notice : this is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B : Enzymatic. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B : Enzymatic, vol. 122, pp. 353-364, 2015. doi : 10.1016/j.molcatb.2015.10.012. |
en_ZA |
dc.subject |
Biochemical characterisation |
en_ZA |
dc.subject |
Cross-linking |
en_ZA |
dc.subject |
Industrial application |
en_ZA |
dc.subject |
Streptomyces |
en_ZA |
dc.subject |
Tyrosinase |
en_ZA |
dc.title |
Partial purification and characterisation of two actinomycete tyrosinases and their application in cross-linking reactions |
en_ZA |
dc.type |
Postprint Article |
en_ZA |