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Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC

The use of bacterial l-asparaginase (LA) is one of the alternative approaches for acrylamide reduction in food stuffs as it catalyzes the conversion of l-asparagine to l-aspartic acid and ammonia. In present investigation, purification of extracellular LA from isolate of Bacillus subtilis sp. strain...

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Autores principales: Sanghvi, Gaurav, Bhimani, Kapil, Vaishnav, Devendra, Oza, Tejas, Dave, Gaurav, Kunjadia, Prashant, Sheth, Navin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4846603/
https://www.ncbi.nlm.nih.gov/pubmed/27186497
http://dx.doi.org/10.1186/s40064-016-2159-8
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author Sanghvi, Gaurav
Bhimani, Kapil
Vaishnav, Devendra
Oza, Tejas
Dave, Gaurav
Kunjadia, Prashant
Sheth, Navin
author_facet Sanghvi, Gaurav
Bhimani, Kapil
Vaishnav, Devendra
Oza, Tejas
Dave, Gaurav
Kunjadia, Prashant
Sheth, Navin
author_sort Sanghvi, Gaurav
collection PubMed
description The use of bacterial l-asparaginase (LA) is one of the alternative approaches for acrylamide reduction in food stuffs as it catalyzes the conversion of l-asparagine to l-aspartic acid and ammonia. In present investigation, purification of extracellular LA from isolate of Bacillus subtilis sp. strain KDPS-1 was carried out by solid state fermentation process. The effects of solid substrates, initial moisture content, moistening agents, temperature, and incubation time on LA production was studied, and the highest asparaginase activity (47 IU/ml) was achieved in the medium having orange peel as substrate. The enzyme was purified to homogeneity by diethylaminoethyl (DEAE) cellulose ion exchange chromatography; with 84.89 % yield and 12.11 fold purity. LA showed stimulant activity against β-mercaptoethanol and was greatly inhibited by Zn(2+) and Hg(2+) metal ions. Reduction of acrylamide in fried potatoes was detected by high performance liquid chromatography, which showed clear degradation of acrylamide by height and area (%) in the chromatograms of standard sample to that of the test sample. Hydrolysates analysis by high performance thin layer chromatography confirmed the test sample to be LA.
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spelling pubmed-48466032016-05-16 Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC Sanghvi, Gaurav Bhimani, Kapil Vaishnav, Devendra Oza, Tejas Dave, Gaurav Kunjadia, Prashant Sheth, Navin Springerplus Research The use of bacterial l-asparaginase (LA) is one of the alternative approaches for acrylamide reduction in food stuffs as it catalyzes the conversion of l-asparagine to l-aspartic acid and ammonia. In present investigation, purification of extracellular LA from isolate of Bacillus subtilis sp. strain KDPS-1 was carried out by solid state fermentation process. The effects of solid substrates, initial moisture content, moistening agents, temperature, and incubation time on LA production was studied, and the highest asparaginase activity (47 IU/ml) was achieved in the medium having orange peel as substrate. The enzyme was purified to homogeneity by diethylaminoethyl (DEAE) cellulose ion exchange chromatography; with 84.89 % yield and 12.11 fold purity. LA showed stimulant activity against β-mercaptoethanol and was greatly inhibited by Zn(2+) and Hg(2+) metal ions. Reduction of acrylamide in fried potatoes was detected by high performance liquid chromatography, which showed clear degradation of acrylamide by height and area (%) in the chromatograms of standard sample to that of the test sample. Hydrolysates analysis by high performance thin layer chromatography confirmed the test sample to be LA. Springer International Publishing 2016-04-26 /pmc/articles/PMC4846603/ /pubmed/27186497 http://dx.doi.org/10.1186/s40064-016-2159-8 Text en © Sanghvi et al. 2016 Open AccessThis article is 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, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Research
Sanghvi, Gaurav
Bhimani, Kapil
Vaishnav, Devendra
Oza, Tejas
Dave, Gaurav
Kunjadia, Prashant
Sheth, Navin
Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC
title Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC
title_full Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC
title_fullStr Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC
title_full_unstemmed Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC
title_short Mitigation of acrylamide by l-asparaginase from Bacillus subtilis KDPS1 and analysis of degradation products by HPLC and HPTLC
title_sort mitigation of acrylamide by l-asparaginase from bacillus subtilis kdps1 and analysis of degradation products by hplc and hptlc
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4846603/
https://www.ncbi.nlm.nih.gov/pubmed/27186497
http://dx.doi.org/10.1186/s40064-016-2159-8
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