Loading…
Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation
In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purifi...
Saved in:
Published in: | Brazilian archives of biology and technology 2011-06, Vol.54 (3), p.559-568 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33 |
---|---|
cites | cdi_FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33 |
container_end_page | 568 |
container_issue | 3 |
container_start_page | 559 |
container_title | Brazilian archives of biology and technology |
container_volume | 54 |
creator | Slivinski, Christiane Trevisan Machado, Alex Vinicius Lopes Iulek, Jorge Ayub, Ricardo Antônio Almeida, Mareci Mendes de |
description | In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively. |
doi_str_mv | 10.1590/S1516-89132011000300018 |
format | article |
fullrecord | <record><control><sourceid>doaj_cross</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_393272619c3547fc8ef18249f44f298f</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_393272619c3547fc8ef18249f44f298f</doaj_id><sourcerecordid>oai_doaj_org_article_393272619c3547fc8ef18249f44f298f</sourcerecordid><originalsourceid>FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33</originalsourceid><addsrcrecordid>eNplkM9OwzAMhysEEmPwDOQFCnGTps1xTPyZNIkDcK4yx-kytcuUdIe9Pd1AExIHy5b96bP0y7J74A9Qav74ASWovNYgCg7AORdjQX2RTc6Hyz_zdXaT0mYkpAI5yTZPPuCaeo-mY7g20eBA0Scz-LBlwTHD2m6PwfSHziRiLoaezdKOYuu7bp_Y1rcU2S4Gu0eybHVgKXTe5mkww4hT7Gk7nGy32ZUzXaK73z7Nvl6eP-dv-fL9dTGfLXOUAEMODnWNSlaOKq7RCCvIVq5UQlgpj0wNXJuitHalCEQFikhhgehEoYwQ02zx47XBbJpd9L2JhyYY35wWIbaNiYPHjhqhRVEVCjSKcnyINTmoC6mdlK7QtRtd1Y8LY0gpkjv7gDfH-JtT_M2_-MU3QI95sw</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation</title><source>SciELO Brazil</source><source>IngentaConnect Journals</source><creator>Slivinski, Christiane Trevisan ; Machado, Alex Vinicius Lopes ; Iulek, Jorge ; Ayub, Ricardo Antônio ; Almeida, Mareci Mendes de</creator><creatorcontrib>Slivinski, Christiane Trevisan ; Machado, Alex Vinicius Lopes ; Iulek, Jorge ; Ayub, Ricardo Antônio ; Almeida, Mareci Mendes de</creatorcontrib><description>In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively.</description><identifier>ISSN: 1516-8913</identifier><identifier>EISSN: 1516-8913</identifier><identifier>EISSN: 1678-4324</identifier><identifier>DOI: 10.1590/S1516-89132011000300018</identifier><language>eng</language><publisher>Instituto de Tecnologia do Paraná (Tecpar)</publisher><subject>Aspergillus niger ; biochemical characterization ; glucoamylase ; purification ; solid-state fermentation</subject><ispartof>Brazilian archives of biology and technology, 2011-06, Vol.54 (3), p.559-568</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33</citedby><cites>FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Slivinski, Christiane Trevisan</creatorcontrib><creatorcontrib>Machado, Alex Vinicius Lopes</creatorcontrib><creatorcontrib>Iulek, Jorge</creatorcontrib><creatorcontrib>Ayub, Ricardo Antônio</creatorcontrib><creatorcontrib>Almeida, Mareci Mendes de</creatorcontrib><title>Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation</title><title>Brazilian archives of biology and technology</title><description>In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively.</description><subject>Aspergillus niger</subject><subject>biochemical characterization</subject><subject>glucoamylase</subject><subject>purification</subject><subject>solid-state fermentation</subject><issn>1516-8913</issn><issn>1516-8913</issn><issn>1678-4324</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNplkM9OwzAMhysEEmPwDOQFCnGTps1xTPyZNIkDcK4yx-kytcuUdIe9Pd1AExIHy5b96bP0y7J74A9Qav74ASWovNYgCg7AORdjQX2RTc6Hyz_zdXaT0mYkpAI5yTZPPuCaeo-mY7g20eBA0Scz-LBlwTHD2m6PwfSHziRiLoaezdKOYuu7bp_Y1rcU2S4Gu0eybHVgKXTe5mkww4hT7Gk7nGy32ZUzXaK73z7Nvl6eP-dv-fL9dTGfLXOUAEMODnWNSlaOKq7RCCvIVq5UQlgpj0wNXJuitHalCEQFikhhgehEoYwQ02zx47XBbJpd9L2JhyYY35wWIbaNiYPHjhqhRVEVCjSKcnyINTmoC6mdlK7QtRtd1Y8LY0gpkjv7gDfH-JtT_M2_-MU3QI95sw</recordid><startdate>20110601</startdate><enddate>20110601</enddate><creator>Slivinski, Christiane Trevisan</creator><creator>Machado, Alex Vinicius Lopes</creator><creator>Iulek, Jorge</creator><creator>Ayub, Ricardo Antônio</creator><creator>Almeida, Mareci Mendes de</creator><general>Instituto de Tecnologia do Paraná (Tecpar)</general><scope>AAYXX</scope><scope>CITATION</scope><scope>DOA</scope></search><sort><creationdate>20110601</creationdate><title>Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation</title><author>Slivinski, Christiane Trevisan ; Machado, Alex Vinicius Lopes ; Iulek, Jorge ; Ayub, Ricardo Antônio ; Almeida, Mareci Mendes de</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Aspergillus niger</topic><topic>biochemical characterization</topic><topic>glucoamylase</topic><topic>purification</topic><topic>solid-state fermentation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Slivinski, Christiane Trevisan</creatorcontrib><creatorcontrib>Machado, Alex Vinicius Lopes</creatorcontrib><creatorcontrib>Iulek, Jorge</creatorcontrib><creatorcontrib>Ayub, Ricardo Antônio</creatorcontrib><creatorcontrib>Almeida, Mareci Mendes de</creatorcontrib><collection>CrossRef</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Brazilian archives of biology and technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Slivinski, Christiane Trevisan</au><au>Machado, Alex Vinicius Lopes</au><au>Iulek, Jorge</au><au>Ayub, Ricardo Antônio</au><au>Almeida, Mareci Mendes de</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation</atitle><jtitle>Brazilian archives of biology and technology</jtitle><date>2011-06-01</date><risdate>2011</risdate><volume>54</volume><issue>3</issue><spage>559</spage><epage>568</epage><pages>559-568</pages><issn>1516-8913</issn><eissn>1516-8913</eissn><eissn>1678-4324</eissn><abstract>In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K M and Vmax were 0.34 mg mL-1 and 160.22 U mL-1, respectively.</abstract><pub>Instituto de Tecnologia do Paraná (Tecpar)</pub><doi>10.1590/S1516-89132011000300018</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1516-8913 |
ispartof | Brazilian archives of biology and technology, 2011-06, Vol.54 (3), p.559-568 |
issn | 1516-8913 1516-8913 1678-4324 |
language | eng |
recordid | cdi_doaj_primary_oai_doaj_org_article_393272619c3547fc8ef18249f44f298f |
source | SciELO Brazil; IngentaConnect Journals |
subjects | Aspergillus niger biochemical characterization glucoamylase purification solid-state fermentation |
title | Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T18%3A20%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-doaj_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biochemical%20characterisation%20of%20a%20glucoamylase%20from%20Aspergillus%20niger%20produced%20by%20solid-state%20fermentation&rft.jtitle=Brazilian%20archives%20of%20biology%20and%20technology&rft.au=Slivinski,%20Christiane%20Trevisan&rft.date=2011-06-01&rft.volume=54&rft.issue=3&rft.spage=559&rft.epage=568&rft.pages=559-568&rft.issn=1516-8913&rft.eissn=1516-8913&rft_id=info:doi/10.1590/S1516-89132011000300018&rft_dat=%3Cdoaj_cross%3Eoai_doaj_org_article_393272619c3547fc8ef18249f44f298f%3C/doaj_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c411t-1fc98c647fe709ca3d3ed7f5633d44c4118109a25ddb6e13716ee6c2ccf326a33%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |