Sago Pith Residue as an Alternative Cheap Substrate for Fermentable Sugars Production
Sago pith residue is one of the most abundant lignocellulosic biomass which can serve as an alternative cheap substrate for fermentable sugars production. This residue is the fibrous waste left behind after the starch extraction process and contains significant amounts of starch (58%), cellulose (23...
Gespeichert in:
Veröffentlicht in: | Applied biochemistry and biotechnology 2012-05, Vol.167 (1), p.122-131 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 131 |
---|---|
container_issue | 1 |
container_start_page | 122 |
container_title | Applied biochemistry and biotechnology |
container_volume | 167 |
creator | Linggang, S. Phang, L. Y. Wasoh, M. H. Abd-Aziz, S. |
description | Sago pith residue is one of the most abundant lignocellulosic biomass which can serve as an alternative cheap substrate for fermentable sugars production. This residue is the fibrous waste left behind after the starch extraction process and contains significant amounts of starch (58%), cellulose (23%), hemicellulose (9.2%) and lignin (3.9%). The conversion of sago pith residue into fermentable sugars is commonly performed using cellulolytic enzymes or known as cellulases. In this study, crude cellulases were produced by two local isolates,
Trichoderma asperellum
UPM1 and
Aspergillus fumigatus
, UPM2 using sago pith residue as substrate.
A. fumigatus
UPM2 gave the highest FPase, CMCase and β-glucosidase activities of 0.39, 23.99 and 0.78 U/ml, respectively, on day 5. The highest activity of FPase, CMCase and β-glucosidase by
T. asperellum
UPM1 was 0.27, 12.03 and 0.42 U/ml, respectively, on day 7. The crude enzyme obtained from
A. fumigatus
UPM2 using β-glucosidase as the rate-limiting enzyme (3.9, 11.7 and 23.4 IU) was used for the saccharification process to convert 5% (w/v) sago pith residue into reducing sugars. Hydrolysis of sago pith residue using crude enzyme containing β-glucosidase with 23.4 IU, produced by
A. fumigatus
UPM2 gave higher reducing sugars production of 20.77 g/l with overall hydrolysis percentage of 73%. |
doi_str_mv | 10.1007/s12010-012-9592-0 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1017984067</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2665981901</sourcerecordid><originalsourceid>FETCH-LOGICAL-c544t-a8dfe050e6b6f4756b6bd994d5561d8837929fffe9cb86881b493ee85ee2d7df3</originalsourceid><addsrcrecordid>eNqN0d9LHDEQB_AgFj1P_wBfJCBCX7ZNsvn5KEdtCwc9qj4v2c3kXNnbPZNswf_eHHtaKQh9mof5zCTMF6FzSr5QQtTXSBmhpCCUFUYYVpADNKNCmIIwQw_RjDBVFoxpc4xOYnwkGWqhjtAxY4JpyeUM3d_a9YBXbXrAvyG2bgRsI7Y9vu4ShN6m9g_gxQPYLb4d65iCTYD9EPANhA30ydYd5M7ahohXYXBjk9qhP0WfvO0inO3rHN3ffLtb_CiWv77_XFwvi0ZwngqrnQciCMhaeq5ELrUzhjshJHVal8ow470H09Raak1rbkoALQCYU86Xc_R52rsNw9MIMVWbNjbQdbaHYYwVJVQZzYlU_0MF48qUPNPLf-jjMOZbdJPKl5e6zIpOqglDjAF8tQ3txobnjKpdPNUUT5WvXu3iqUieudhvHusNuLeJ1zwyuNoDGxvb-WD7po1_nTCS6ZJlxyYXc6tfQ3j_xY9efwHsXqXi</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1015007683</pqid></control><display><type>article</type><title>Sago Pith Residue as an Alternative Cheap Substrate for Fermentable Sugars Production</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Linggang, S. ; Phang, L. Y. ; Wasoh, M. H. ; Abd-Aziz, S.</creator><creatorcontrib>Linggang, S. ; Phang, L. Y. ; Wasoh, M. H. ; Abd-Aziz, S.</creatorcontrib><description>Sago pith residue is one of the most abundant lignocellulosic biomass which can serve as an alternative cheap substrate for fermentable sugars production. This residue is the fibrous waste left behind after the starch extraction process and contains significant amounts of starch (58%), cellulose (23%), hemicellulose (9.2%) and lignin (3.9%). The conversion of sago pith residue into fermentable sugars is commonly performed using cellulolytic enzymes or known as cellulases. In this study, crude cellulases were produced by two local isolates,
Trichoderma asperellum
UPM1 and
Aspergillus fumigatus
, UPM2 using sago pith residue as substrate.
A. fumigatus
UPM2 gave the highest FPase, CMCase and β-glucosidase activities of 0.39, 23.99 and 0.78 U/ml, respectively, on day 5. The highest activity of FPase, CMCase and β-glucosidase by
T. asperellum
UPM1 was 0.27, 12.03 and 0.42 U/ml, respectively, on day 7. The crude enzyme obtained from
A. fumigatus
UPM2 using β-glucosidase as the rate-limiting enzyme (3.9, 11.7 and 23.4 IU) was used for the saccharification process to convert 5% (w/v) sago pith residue into reducing sugars. Hydrolysis of sago pith residue using crude enzyme containing β-glucosidase with 23.4 IU, produced by
A. fumigatus
UPM2 gave higher reducing sugars production of 20.77 g/l with overall hydrolysis percentage of 73%.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-012-9592-0</identifier><identifier>PMID: 22528646</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>New York: Springer-Verlag</publisher><subject>Aspergillus fumigatus ; Aspergillus fumigatus - enzymology ; Biocatalysis ; Biochemistry ; Biological and medical sciences ; Biotechnology ; Cellulases - metabolism ; Cellulose ; Chemistry ; Chemistry and Materials Science ; Fermentation ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - metabolism ; Hydrolysis ; Industrial Waste - analysis ; Lignin - metabolism ; Residues ; Starch ; Substrates ; Sugar ; Trichoderma ; Trichoderma - enzymology</subject><ispartof>Applied biochemistry and biotechnology, 2012-05, Vol.167 (1), p.122-131</ispartof><rights>Springer Science+Business Media, LLC 2012</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-a8dfe050e6b6f4756b6bd994d5561d8837929fffe9cb86881b493ee85ee2d7df3</citedby><cites>FETCH-LOGICAL-c544t-a8dfe050e6b6f4756b6bd994d5561d8837929fffe9cb86881b493ee85ee2d7df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-012-9592-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-012-9592-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25962832$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22528646$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Linggang, S.</creatorcontrib><creatorcontrib>Phang, L. Y.</creatorcontrib><creatorcontrib>Wasoh, M. H.</creatorcontrib><creatorcontrib>Abd-Aziz, S.</creatorcontrib><title>Sago Pith Residue as an Alternative Cheap Substrate for Fermentable Sugars Production</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Sago pith residue is one of the most abundant lignocellulosic biomass which can serve as an alternative cheap substrate for fermentable sugars production. This residue is the fibrous waste left behind after the starch extraction process and contains significant amounts of starch (58%), cellulose (23%), hemicellulose (9.2%) and lignin (3.9%). The conversion of sago pith residue into fermentable sugars is commonly performed using cellulolytic enzymes or known as cellulases. In this study, crude cellulases were produced by two local isolates,
Trichoderma asperellum
UPM1 and
Aspergillus fumigatus
, UPM2 using sago pith residue as substrate.
A. fumigatus
UPM2 gave the highest FPase, CMCase and β-glucosidase activities of 0.39, 23.99 and 0.78 U/ml, respectively, on day 5. The highest activity of FPase, CMCase and β-glucosidase by
T. asperellum
UPM1 was 0.27, 12.03 and 0.42 U/ml, respectively, on day 7. The crude enzyme obtained from
A. fumigatus
UPM2 using β-glucosidase as the rate-limiting enzyme (3.9, 11.7 and 23.4 IU) was used for the saccharification process to convert 5% (w/v) sago pith residue into reducing sugars. Hydrolysis of sago pith residue using crude enzyme containing β-glucosidase with 23.4 IU, produced by
A. fumigatus
UPM2 gave higher reducing sugars production of 20.77 g/l with overall hydrolysis percentage of 73%.</description><subject>Aspergillus fumigatus</subject><subject>Aspergillus fumigatus - enzymology</subject><subject>Biocatalysis</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cellulases - metabolism</subject><subject>Cellulose</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Fermentation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - metabolism</subject><subject>Hydrolysis</subject><subject>Industrial Waste - analysis</subject><subject>Lignin - metabolism</subject><subject>Residues</subject><subject>Starch</subject><subject>Substrates</subject><subject>Sugar</subject><subject>Trichoderma</subject><subject>Trichoderma - enzymology</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqN0d9LHDEQB_AgFj1P_wBfJCBCX7ZNsvn5KEdtCwc9qj4v2c3kXNnbPZNswf_eHHtaKQh9mof5zCTMF6FzSr5QQtTXSBmhpCCUFUYYVpADNKNCmIIwQw_RjDBVFoxpc4xOYnwkGWqhjtAxY4JpyeUM3d_a9YBXbXrAvyG2bgRsI7Y9vu4ShN6m9g_gxQPYLb4d65iCTYD9EPANhA30ydYd5M7ahohXYXBjk9qhP0WfvO0inO3rHN3ffLtb_CiWv77_XFwvi0ZwngqrnQciCMhaeq5ELrUzhjshJHVal8ow470H09Raak1rbkoALQCYU86Xc_R52rsNw9MIMVWbNjbQdbaHYYwVJVQZzYlU_0MF48qUPNPLf-jjMOZbdJPKl5e6zIpOqglDjAF8tQ3txobnjKpdPNUUT5WvXu3iqUieudhvHusNuLeJ1zwyuNoDGxvb-WD7po1_nTCS6ZJlxyYXc6tfQ3j_xY9efwHsXqXi</recordid><startdate>20120501</startdate><enddate>20120501</enddate><creator>Linggang, S.</creator><creator>Phang, L. Y.</creator><creator>Wasoh, M. H.</creator><creator>Abd-Aziz, S.</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20120501</creationdate><title>Sago Pith Residue as an Alternative Cheap Substrate for Fermentable Sugars Production</title><author>Linggang, S. ; Phang, L. Y. ; Wasoh, M. H. ; Abd-Aziz, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-a8dfe050e6b6f4756b6bd994d5561d8837929fffe9cb86881b493ee85ee2d7df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Aspergillus fumigatus</topic><topic>Aspergillus fumigatus - enzymology</topic><topic>Biocatalysis</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cellulases - metabolism</topic><topic>Cellulose</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Fermentation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - metabolism</topic><topic>Hydrolysis</topic><topic>Industrial Waste - analysis</topic><topic>Lignin - metabolism</topic><topic>Residues</topic><topic>Starch</topic><topic>Substrates</topic><topic>Sugar</topic><topic>Trichoderma</topic><topic>Trichoderma - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Linggang, S.</creatorcontrib><creatorcontrib>Phang, L. Y.</creatorcontrib><creatorcontrib>Wasoh, M. H.</creatorcontrib><creatorcontrib>Abd-Aziz, S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Linggang, S.</au><au>Phang, L. Y.</au><au>Wasoh, M. H.</au><au>Abd-Aziz, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sago Pith Residue as an Alternative Cheap Substrate for Fermentable Sugars Production</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2012-05-01</date><risdate>2012</risdate><volume>167</volume><issue>1</issue><spage>122</spage><epage>131</epage><pages>122-131</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>Sago pith residue is one of the most abundant lignocellulosic biomass which can serve as an alternative cheap substrate for fermentable sugars production. This residue is the fibrous waste left behind after the starch extraction process and contains significant amounts of starch (58%), cellulose (23%), hemicellulose (9.2%) and lignin (3.9%). The conversion of sago pith residue into fermentable sugars is commonly performed using cellulolytic enzymes or known as cellulases. In this study, crude cellulases were produced by two local isolates,
Trichoderma asperellum
UPM1 and
Aspergillus fumigatus
, UPM2 using sago pith residue as substrate.
A. fumigatus
UPM2 gave the highest FPase, CMCase and β-glucosidase activities of 0.39, 23.99 and 0.78 U/ml, respectively, on day 5. The highest activity of FPase, CMCase and β-glucosidase by
T. asperellum
UPM1 was 0.27, 12.03 and 0.42 U/ml, respectively, on day 7. The crude enzyme obtained from
A. fumigatus
UPM2 using β-glucosidase as the rate-limiting enzyme (3.9, 11.7 and 23.4 IU) was used for the saccharification process to convert 5% (w/v) sago pith residue into reducing sugars. Hydrolysis of sago pith residue using crude enzyme containing β-glucosidase with 23.4 IU, produced by
A. fumigatus
UPM2 gave higher reducing sugars production of 20.77 g/l with overall hydrolysis percentage of 73%.</abstract><cop>New York</cop><pub>Springer-Verlag</pub><pmid>22528646</pmid><doi>10.1007/s12010-012-9592-0</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0273-2289 |
ispartof | Applied biochemistry and biotechnology, 2012-05, Vol.167 (1), p.122-131 |
issn | 0273-2289 1559-0291 |
language | eng |
recordid | cdi_proquest_miscellaneous_1017984067 |
source | MEDLINE; SpringerLink Journals |
subjects | Aspergillus fumigatus Aspergillus fumigatus - enzymology Biocatalysis Biochemistry Biological and medical sciences Biotechnology Cellulases - metabolism Cellulose Chemistry Chemistry and Materials Science Fermentation Fundamental and applied biological sciences. Psychology Fungal Proteins - metabolism Hydrolysis Industrial Waste - analysis Lignin - metabolism Residues Starch Substrates Sugar Trichoderma Trichoderma - enzymology |
title | Sago Pith Residue as an Alternative Cheap Substrate for Fermentable Sugars Production |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-20T00%3A02%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Sago%20Pith%20Residue%20as%20an%20Alternative%20Cheap%20Substrate%20for%20Fermentable%20Sugars%20Production&rft.jtitle=Applied%20biochemistry%20and%20biotechnology&rft.au=Linggang,%20S.&rft.date=2012-05-01&rft.volume=167&rft.issue=1&rft.spage=122&rft.epage=131&rft.pages=122-131&rft.issn=0273-2289&rft.eissn=1559-0291&rft.coden=ABIBDL&rft_id=info:doi/10.1007/s12010-012-9592-0&rft_dat=%3Cproquest_cross%3E2665981901%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1015007683&rft_id=info:pmid/22528646&rfr_iscdi=true |