Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data

Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available...
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Autor*in:	de Freitas, Marcela Medeiros [verfasserIn] Souza, Paula Monteiro Cruvinel, Kellen Barros, Thais Santos, Suikinai Nobre Long, Paul F. Pessoa, Adalberto Magalhães, Pérola Oliveira

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	-Asparaginase Enzyme assay Nessler method Interferences

Anmerkung:	© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 103(2019), 13 vom: 18. Mai, Seite 5161-5166
Übergeordnetes Werk:	volume:103 ; year:2019 ; number:13 ; day:18 ; month:05 ; pages:5161-5166

Links:	Volltext

DOI / URN:	10.1007/s00253-019-09890-0

Katalog-ID:	SPR003034542

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520			\|a Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia.
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allfields	10.1007/s00253-019-09890-0 doi (DE-627)SPR003034542 (SPR)s00253-019-09890-0-e DE-627 ger DE-627 rakwb eng de Freitas, Marcela Medeiros verfasserin aut Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. -Asparaginase (dpeaa)DE-He213 Enzyme assay (dpeaa)DE-He213 Nessler method (dpeaa)DE-He213 Interferences (dpeaa)DE-He213 Souza, Paula Monteiro aut Cruvinel, Kellen aut Barros, Thais aut Santos, Suikinai Nobre aut Long, Paul F. aut Pessoa, Adalberto aut Magalhães, Pérola Oliveira (orcid)0000-0001-8011-6940 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 103(2019), 13 vom: 18. Mai, Seite 5161-5166 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166 https://dx.doi.org/10.1007/s00253-019-09890-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 103 2019 13 18 05 5161-5166
spelling	10.1007/s00253-019-09890-0 doi (DE-627)SPR003034542 (SPR)s00253-019-09890-0-e DE-627 ger DE-627 rakwb eng de Freitas, Marcela Medeiros verfasserin aut Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. -Asparaginase (dpeaa)DE-He213 Enzyme assay (dpeaa)DE-He213 Nessler method (dpeaa)DE-He213 Interferences (dpeaa)DE-He213 Souza, Paula Monteiro aut Cruvinel, Kellen aut Barros, Thais aut Santos, Suikinai Nobre aut Long, Paul F. aut Pessoa, Adalberto aut Magalhães, Pérola Oliveira (orcid)0000-0001-8011-6940 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 103(2019), 13 vom: 18. Mai, Seite 5161-5166 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166 https://dx.doi.org/10.1007/s00253-019-09890-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 103 2019 13 18 05 5161-5166
allfields_unstemmed	10.1007/s00253-019-09890-0 doi (DE-627)SPR003034542 (SPR)s00253-019-09890-0-e DE-627 ger DE-627 rakwb eng de Freitas, Marcela Medeiros verfasserin aut Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. -Asparaginase (dpeaa)DE-He213 Enzyme assay (dpeaa)DE-He213 Nessler method (dpeaa)DE-He213 Interferences (dpeaa)DE-He213 Souza, Paula Monteiro aut Cruvinel, Kellen aut Barros, Thais aut Santos, Suikinai Nobre aut Long, Paul F. aut Pessoa, Adalberto aut Magalhães, Pérola Oliveira (orcid)0000-0001-8011-6940 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 103(2019), 13 vom: 18. Mai, Seite 5161-5166 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166 https://dx.doi.org/10.1007/s00253-019-09890-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 103 2019 13 18 05 5161-5166
allfieldsGer	10.1007/s00253-019-09890-0 doi (DE-627)SPR003034542 (SPR)s00253-019-09890-0-e DE-627 ger DE-627 rakwb eng de Freitas, Marcela Medeiros verfasserin aut Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. -Asparaginase (dpeaa)DE-He213 Enzyme assay (dpeaa)DE-He213 Nessler method (dpeaa)DE-He213 Interferences (dpeaa)DE-He213 Souza, Paula Monteiro aut Cruvinel, Kellen aut Barros, Thais aut Santos, Suikinai Nobre aut Long, Paul F. aut Pessoa, Adalberto aut Magalhães, Pérola Oliveira (orcid)0000-0001-8011-6940 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 103(2019), 13 vom: 18. Mai, Seite 5161-5166 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166 https://dx.doi.org/10.1007/s00253-019-09890-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 103 2019 13 18 05 5161-5166
allfieldsSound	10.1007/s00253-019-09890-0 doi (DE-627)SPR003034542 (SPR)s00253-019-09890-0-e DE-627 ger DE-627 rakwb eng de Freitas, Marcela Medeiros verfasserin aut Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. -Asparaginase (dpeaa)DE-He213 Enzyme assay (dpeaa)DE-He213 Nessler method (dpeaa)DE-He213 Interferences (dpeaa)DE-He213 Souza, Paula Monteiro aut Cruvinel, Kellen aut Barros, Thais aut Santos, Suikinai Nobre aut Long, Paul F. aut Pessoa, Adalberto aut Magalhães, Pérola Oliveira (orcid)0000-0001-8011-6940 aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 103(2019), 13 vom: 18. Mai, Seite 5161-5166 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166 https://dx.doi.org/10.1007/s00253-019-09890-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 103 2019 13 18 05 5161-5166
language	English
source	Enthalten in Applied microbiology and biotechnology 103(2019), 13 vom: 18. Mai, Seite 5161-5166 volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166
sourceStr	Enthalten in Applied microbiology and biotechnology 103(2019), 13 vom: 18. Mai, Seite 5161-5166 volume:103 year:2019 number:13 day:18 month:05 pages:5161-5166
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	-Asparaginase Enzyme assay Nessler method Interferences
isfreeaccess_bool	false
container_title	Applied microbiology and biotechnology
authorswithroles_txt_mv	de Freitas, Marcela Medeiros @@aut@@ Souza, Paula Monteiro @@aut@@ Cruvinel, Kellen @@aut@@ Barros, Thais @@aut@@ Santos, Suikinai Nobre @@aut@@ Long, Paul F. @@aut@@ Pessoa, Adalberto @@aut@@ Magalhães, Pérola Oliveira @@aut@@
publishDateDaySort_date	2019-05-18T00:00:00Z
hierarchy_top_id	265509564
id	SPR003034542
language_de	englisch
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author	de Freitas, Marcela Medeiros
spellingShingle	de Freitas, Marcela Medeiros misc -Asparaginase misc Enzyme assay misc Nessler method misc Interferences Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
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topic_title	Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data -Asparaginase (dpeaa)DE-He213 Enzyme assay (dpeaa)DE-He213 Nessler method (dpeaa)DE-He213 Interferences (dpeaa)DE-He213
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title	Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
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title_full	Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
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author_browse	de Freitas, Marcela Medeiros Souza, Paula Monteiro Cruvinel, Kellen Barros, Thais Santos, Suikinai Nobre Long, Paul F. Pessoa, Adalberto Magalhães, Pérola Oliveira
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title_sort	interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
title_auth	Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
abstract	Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. © Springer-Verlag GmbH Germany, part of Springer Nature 2019
abstractGer	Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. © Springer-Verlag GmbH Germany, part of Springer Nature 2019
abstract_unstemmed	Abstract l-asparaginase is an enzyme produced by microorganisms, plants, and animals, which is used clinically for the treatment for acute lymphoblastic leukemia (ALL) and, in the food industry, to control acrylamide formation in baked foods. The purpose of this review was to evaluate the available literature regarding microbial sources of l-asparaginase, culture media used to achieve maximum enzyme expression in microbial fermentations, and assay methods employed to assess l-asparaginase activity. Studies were gathered by searching PubMed, and Web of Science databases before January 22, 2018, with no time restrictions. The articles were evaluated according to the source of l-asparaginase being studied, the nitrogen source in the culture medium, the type of sample, and the method employed to evaluate l-asparaginase activity. Bacterial l-asparaginase appeared to be the most commonly studied source of the enzyme and, most often, the enzyme activity was assayed from crude protein extracts using the Nessler method, which is an indirect measurement of asparaginase activity that determines the concentration of ammonia generated after the action of the enzyme on the substrate, l-asparagine. However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. We suggest that current estimates of l-asparaginase activity reported in the literature may be overestimated when Nessler reagent is used, since we were unable to find a single study that made reference to the possible inference of fermentation derived ammonia. © Springer-Verlag GmbH Germany, part of Springer Nature 2019
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title_short	Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
url	https://dx.doi.org/10.1007/s00253-019-09890-0
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up_date	2024-07-03T16:53:09.275Z
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However, ammonia is also generated throughout microbial fermentations and this endogenous ammonia will also reduce the Nessler reagent if crude microbial extracts are used to determine total l-asparaginase activity. 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