Loading…

Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation

•Protein isolates were obtained from basil seed by isoelectric precipitation.•HPLC analysis showed abundance of glutamic acid, threonine, and arginine.•Electrophoretic bands were observed in the range of 11.5 to 77.6 kDa.•FTIR showed characteristic peaks for amide I, amide II, and amide III.•DSC ana...

Full description

Saved in:
Bibliographic Details
Published in:Food chemistry advances 2023-12, Vol.3, p.100424, Article 100424
Main Authors: Nazir, Sadaf, Wani, Idrees Ahmed
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-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923
cites cdi_FETCH-LOGICAL-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923
container_end_page
container_issue
container_start_page 100424
container_title Food chemistry advances
container_volume 3
creator Nazir, Sadaf
Wani, Idrees Ahmed
description •Protein isolates were obtained from basil seed by isoelectric precipitation.•HPLC analysis showed abundance of glutamic acid, threonine, and arginine.•Electrophoretic bands were observed in the range of 11.5 to 77.6 kDa.•FTIR showed characteristic peaks for amide I, amide II, and amide III.•DSC analysis showed denaturation temperature (Tp) was 95.34 °C. Protein was isolated by isoelectric precipitation from basil seeds (after mucilage and oil extraction) and investigated for its physicochemical and functional properties. The protein content of basil seed protein isolate (BPI) was 89.08%. High performance liquid chromatography (HPLC) showed presence of essential amino acids. Glutamic acid (17.40%), threonine (13.65%), and arginine (11.32%) were abundant. Sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE) analysis showed molecular weights in the range of 11.5 to 77.6 kDa. Differential scanning calorimetry (DSC) of basil seed protein isolate revealed a high denaturation temperature (95.34 °C). The Fourier transform infrared spectroscopy (FTIR) indicated presence of amide I, II, and III groups. Characteristic peaks for β- sheet conformation were also observed. Results showed that BPI had high emulsifying ability index (298.4 m2/g) at pH 10. Solubility was lowest at pH 9 (10.69%). Functional properties such as protein solubility, foaming, and emulsification properties were high at pH 10. An increasing trend was observed from pH 2 to 5. High bulk density (0.799 g/ mL) and low water absorption capacity (0.51 g/ g) was observed.
doi_str_mv 10.1016/j.focha.2023.100424
format article
fullrecord <record><control><sourceid>elsevier_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_afd711ba56a74708836e6686af4e0239</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S2772753X23002459</els_id><doaj_id>oai_doaj_org_article_afd711ba56a74708836e6686af4e0239</doaj_id><sourcerecordid>S2772753X23002459</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923</originalsourceid><addsrcrecordid>eNp9kE1LAzEQhhdRULS_wMse9dA12aSbXcGDiB-FQntQ8BZmJ5M2ZbuRZCv4701bEU-eMnnhfTJ5suySs4IzXt2sC-txBUXJSpESJkt5lJ2VSpVjNRHvx3_m02wU45oxVtacC67OsuUi-IFcn7voOxgot8Fv8hai6_JIZGJ-NUe32f5kDtM0K65v88XqKzpMD9PGIXQ59Ca32x4H5_t0TQsFwIGCi7CLLrITC12k0c95nr09Pb4-vIxn8-fpw_1sjKJs5LgxlrccsOVMGomsbiSzvGGihrbiSkwAuVFGCmVsxVHaFqwhI2pRVbVqSnGeTQ9c42GtP4LbQPjSHpzeBz4sNYTBYUc6NRXnLUwqUFKxOjEoUSqwkpLKJrHEgYXBxxjI_vI40zv1eq336vVOvT6oT627Q4vSNz8dBR3RUY9kXCAc0h7u3_43HACNvA</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation</title><source>ScienceDirect</source><creator>Nazir, Sadaf ; Wani, Idrees Ahmed</creator><creatorcontrib>Nazir, Sadaf ; Wani, Idrees Ahmed</creatorcontrib><description>•Protein isolates were obtained from basil seed by isoelectric precipitation.•HPLC analysis showed abundance of glutamic acid, threonine, and arginine.•Electrophoretic bands were observed in the range of 11.5 to 77.6 kDa.•FTIR showed characteristic peaks for amide I, amide II, and amide III.•DSC analysis showed denaturation temperature (Tp) was 95.34 °C. Protein was isolated by isoelectric precipitation from basil seeds (after mucilage and oil extraction) and investigated for its physicochemical and functional properties. The protein content of basil seed protein isolate (BPI) was 89.08%. High performance liquid chromatography (HPLC) showed presence of essential amino acids. Glutamic acid (17.40%), threonine (13.65%), and arginine (11.32%) were abundant. Sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE) analysis showed molecular weights in the range of 11.5 to 77.6 kDa. Differential scanning calorimetry (DSC) of basil seed protein isolate revealed a high denaturation temperature (95.34 °C). The Fourier transform infrared spectroscopy (FTIR) indicated presence of amide I, II, and III groups. Characteristic peaks for β- sheet conformation were also observed. Results showed that BPI had high emulsifying ability index (298.4 m2/g) at pH 10. Solubility was lowest at pH 9 (10.69%). Functional properties such as protein solubility, foaming, and emulsification properties were high at pH 10. An increasing trend was observed from pH 2 to 5. High bulk density (0.799 g/ mL) and low water absorption capacity (0.51 g/ g) was observed.</description><identifier>ISSN: 2772-753X</identifier><identifier>EISSN: 2772-753X</identifier><identifier>DOI: 10.1016/j.focha.2023.100424</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Amino-acids ; Functional properties ; Isoelectric precipitation ; Plant protein</subject><ispartof>Food chemistry advances, 2023-12, Vol.3, p.100424, Article 100424</ispartof><rights>2023 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923</citedby><cites>FETCH-LOGICAL-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S2772753X23002459$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,3538,27911,27912,45767</link.rule.ids></links><search><creatorcontrib>Nazir, Sadaf</creatorcontrib><creatorcontrib>Wani, Idrees Ahmed</creatorcontrib><title>Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation</title><title>Food chemistry advances</title><description>•Protein isolates were obtained from basil seed by isoelectric precipitation.•HPLC analysis showed abundance of glutamic acid, threonine, and arginine.•Electrophoretic bands were observed in the range of 11.5 to 77.6 kDa.•FTIR showed characteristic peaks for amide I, amide II, and amide III.•DSC analysis showed denaturation temperature (Tp) was 95.34 °C. Protein was isolated by isoelectric precipitation from basil seeds (after mucilage and oil extraction) and investigated for its physicochemical and functional properties. The protein content of basil seed protein isolate (BPI) was 89.08%. High performance liquid chromatography (HPLC) showed presence of essential amino acids. Glutamic acid (17.40%), threonine (13.65%), and arginine (11.32%) were abundant. Sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE) analysis showed molecular weights in the range of 11.5 to 77.6 kDa. Differential scanning calorimetry (DSC) of basil seed protein isolate revealed a high denaturation temperature (95.34 °C). The Fourier transform infrared spectroscopy (FTIR) indicated presence of amide I, II, and III groups. Characteristic peaks for β- sheet conformation were also observed. Results showed that BPI had high emulsifying ability index (298.4 m2/g) at pH 10. Solubility was lowest at pH 9 (10.69%). Functional properties such as protein solubility, foaming, and emulsification properties were high at pH 10. An increasing trend was observed from pH 2 to 5. High bulk density (0.799 g/ mL) and low water absorption capacity (0.51 g/ g) was observed.</description><subject>Amino-acids</subject><subject>Functional properties</subject><subject>Isoelectric precipitation</subject><subject>Plant protein</subject><issn>2772-753X</issn><issn>2772-753X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNp9kE1LAzEQhhdRULS_wMse9dA12aSbXcGDiB-FQntQ8BZmJ5M2ZbuRZCv4701bEU-eMnnhfTJ5suySs4IzXt2sC-txBUXJSpESJkt5lJ2VSpVjNRHvx3_m02wU45oxVtacC67OsuUi-IFcn7voOxgot8Fv8hai6_JIZGJ-NUe32f5kDtM0K65v88XqKzpMD9PGIXQ59Ca32x4H5_t0TQsFwIGCi7CLLrITC12k0c95nr09Pb4-vIxn8-fpw_1sjKJs5LgxlrccsOVMGomsbiSzvGGihrbiSkwAuVFGCmVsxVHaFqwhI2pRVbVqSnGeTQ9c42GtP4LbQPjSHpzeBz4sNYTBYUc6NRXnLUwqUFKxOjEoUSqwkpLKJrHEgYXBxxjI_vI40zv1eq336vVOvT6oT627Q4vSNz8dBR3RUY9kXCAc0h7u3_43HACNvA</recordid><startdate>202312</startdate><enddate>202312</enddate><creator>Nazir, Sadaf</creator><creator>Wani, Idrees Ahmed</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>DOA</scope></search><sort><creationdate>202312</creationdate><title>Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation</title><author>Nazir, Sadaf ; Wani, Idrees Ahmed</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Amino-acids</topic><topic>Functional properties</topic><topic>Isoelectric precipitation</topic><topic>Plant protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nazir, Sadaf</creatorcontrib><creatorcontrib>Wani, Idrees Ahmed</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>CrossRef</collection><collection>Directory of Open Access Journals</collection><jtitle>Food chemistry advances</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nazir, Sadaf</au><au>Wani, Idrees Ahmed</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation</atitle><jtitle>Food chemistry advances</jtitle><date>2023-12</date><risdate>2023</risdate><volume>3</volume><spage>100424</spage><pages>100424-</pages><artnum>100424</artnum><issn>2772-753X</issn><eissn>2772-753X</eissn><abstract>•Protein isolates were obtained from basil seed by isoelectric precipitation.•HPLC analysis showed abundance of glutamic acid, threonine, and arginine.•Electrophoretic bands were observed in the range of 11.5 to 77.6 kDa.•FTIR showed characteristic peaks for amide I, amide II, and amide III.•DSC analysis showed denaturation temperature (Tp) was 95.34 °C. Protein was isolated by isoelectric precipitation from basil seeds (after mucilage and oil extraction) and investigated for its physicochemical and functional properties. The protein content of basil seed protein isolate (BPI) was 89.08%. High performance liquid chromatography (HPLC) showed presence of essential amino acids. Glutamic acid (17.40%), threonine (13.65%), and arginine (11.32%) were abundant. Sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE) analysis showed molecular weights in the range of 11.5 to 77.6 kDa. Differential scanning calorimetry (DSC) of basil seed protein isolate revealed a high denaturation temperature (95.34 °C). The Fourier transform infrared spectroscopy (FTIR) indicated presence of amide I, II, and III groups. Characteristic peaks for β- sheet conformation were also observed. Results showed that BPI had high emulsifying ability index (298.4 m2/g) at pH 10. Solubility was lowest at pH 9 (10.69%). Functional properties such as protein solubility, foaming, and emulsification properties were high at pH 10. An increasing trend was observed from pH 2 to 5. High bulk density (0.799 g/ mL) and low water absorption capacity (0.51 g/ g) was observed.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.focha.2023.100424</doi><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2772-753X
ispartof Food chemistry advances, 2023-12, Vol.3, p.100424, Article 100424
issn 2772-753X
2772-753X
language eng
recordid cdi_doaj_primary_oai_doaj_org_article_afd711ba56a74708836e6686af4e0239
source ScienceDirect
subjects Amino-acids
Functional properties
Isoelectric precipitation
Plant protein
title Protein isolate from basil seeds (Ocimum basilicum L.): Physicochemical and functional characterisation
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T21%3A01%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-elsevier_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%20isolate%20from%20basil%20seeds%20(Ocimum%20basilicum%20L.):%20Physicochemical%20and%20functional%20characterisation&rft.jtitle=Food%20chemistry%20advances&rft.au=Nazir,%20Sadaf&rft.date=2023-12&rft.volume=3&rft.spage=100424&rft.pages=100424-&rft.artnum=100424&rft.issn=2772-753X&rft.eissn=2772-753X&rft_id=info:doi/10.1016/j.focha.2023.100424&rft_dat=%3Celsevier_doaj_%3ES2772753X23002459%3C/elsevier_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3294-9df1b1acb104d4c08940f19038ab61735ac1d7d437df61c4fbafded3836687923%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