Jojoba Seed Meal Proteins Associated with Proteolytic and Protease Inhibitory Activities
The jojoba, Simmondsia chinensis, is a characteristic desert plant native to the Sonoran desert. The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-in...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2002-09, Vol.50 (20), p.5670-5675 |
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| container_end_page | 5675 |
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| container_issue | 20 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Shrestha, Madan K Peri, Irena Smirnoff, Patricia Birk, Yehudith Golan-Goldhirsh, Avi |
| description | The jojoba, Simmondsia chinensis, is a characteristic desert plant native to the Sonoran desert. The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-inhibitory activity. SDS−PAGE showed two major proteins at 50 kDa and 25 kDa both in the albumins and in the globulins. The 25 kDa protein has trypsin- and chymotrypsin-inhibitory activities. In vitro digestibility of the globulins and albumins resembled that of casein and soybean protein concentrates and was increased after heat treatment. The increased digestibility achieved by boiling may be attributed to inactivation of the protease inhibitors and denaturation of proteins. Keywords: Jojoba meal protein; Simmondsia chinensis; solubility; protease inhibitory activity; digestibility |
| doi_str_mv | 10.1021/jf020161h |
| format | Article |
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The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-inhibitory activity. SDS−PAGE showed two major proteins at 50 kDa and 25 kDa both in the albumins and in the globulins. The 25 kDa protein has trypsin- and chymotrypsin-inhibitory activities. In vitro digestibility of the globulins and albumins resembled that of casein and soybean protein concentrates and was increased after heat treatment. The increased digestibility achieved by boiling may be attributed to inactivation of the protease inhibitors and denaturation of proteins. 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Psychology ; Globulins - analysis ; Globulins - metabolism ; Magnoliopsida - chemistry ; Molecular Weight ; Plant Extracts - chemistry ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plant Proteins - pharmacology ; Protease Inhibitors - analysis ; Protease Inhibitors - pharmacology ; Seeds - chemistry</subject><ispartof>Journal of agricultural and food chemistry, 2002-09, Vol.50 (20), p.5670-5675</ispartof><rights>Copyright © 2002 American Chemical Society</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a379t-5767f97867b7deca7fbc24694917e80ad35613ce87d59e5cb855c3f4dfe071fa3</citedby><cites>FETCH-LOGICAL-a379t-5767f97867b7deca7fbc24694917e80ad35613ce87d59e5cb855c3f4dfe071fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf020161h$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf020161h$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13936880$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12236696$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shrestha, Madan K</creatorcontrib><creatorcontrib>Peri, Irena</creatorcontrib><creatorcontrib>Smirnoff, Patricia</creatorcontrib><creatorcontrib>Birk, Yehudith</creatorcontrib><creatorcontrib>Golan-Goldhirsh, Avi</creatorcontrib><title>Jojoba Seed Meal Proteins Associated with Proteolytic and Protease Inhibitory Activities</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The jojoba, Simmondsia chinensis, is a characteristic desert plant native to the Sonoran desert. The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-inhibitory activity. SDS−PAGE showed two major proteins at 50 kDa and 25 kDa both in the albumins and in the globulins. The 25 kDa protein has trypsin- and chymotrypsin-inhibitory activities. In vitro digestibility of the globulins and albumins resembled that of casein and soybean protein concentrates and was increased after heat treatment. The increased digestibility achieved by boiling may be attributed to inactivation of the protease inhibitors and denaturation of proteins. Keywords: Jojoba meal protein; Simmondsia chinensis; solubility; protease inhibitory activity; digestibility</description><subject>Albumins - analysis</subject><subject>Albumins - metabolism</subject><subject>Amino Acids - analysis</subject><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>Biological and medical sciences</subject><subject>Chemical Fractionation</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endopeptidases - analysis</subject><subject>Endopeptidases - metabolism</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Globulins - analysis</subject><subject>Globulins - metabolism</subject><subject>Magnoliopsida - chemistry</subject><subject>Molecular Weight</subject><subject>Plant Extracts - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Proteins - pharmacology</subject><subject>Protease Inhibitors - analysis</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Seeds - chemistry</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0EtPGzEUBWCroiqBdtE_gGYDEosp9jh-zDJChdLyUkMldtYdz7XiMBlT26HNv-9UE5ENK8s6n46uDiGfGf3CaMXOlo5WlEm2eEcmTFS0FIzpPTKhQ1hqIdk-OUhpSSnVQtEPZJ9VFZeylhPy-D0sQwPFHLEtbhC64j6GjL5PxSylYD3kIfjj82IMQrfJ3hbQt-MfEhZX_cI3Poe4KWY2-xefPaaP5L2DLuGn7XtIfl18fTj_Vl7fXV6dz65L4KrOpVBSuVppqRrVogXlGltNZT2tmUJNoeXD-dyiVq2oUdhGC2G5m7YOqWIO-CE5GXufY_i9xpTNyieLXQc9hnUyqqK1Fno6wNMR2hhSiujMc_QriBvDqPk_o3mdcbBH29J1s8J2J7e7DeB4CyBZ6FyE3vq0c7zmUms6uHJ0PmX8-5pDfDJScSXMw_3c3DzOf_y8pZfmYtcLNpllWMd-2O6NA_8BXOiVuA</recordid><startdate>20020925</startdate><enddate>20020925</enddate><creator>Shrestha, Madan K</creator><creator>Peri, Irena</creator><creator>Smirnoff, Patricia</creator><creator>Birk, Yehudith</creator><creator>Golan-Goldhirsh, Avi</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>20020925</creationdate><title>Jojoba Seed Meal Proteins Associated with Proteolytic and Protease Inhibitory Activities</title><author>Shrestha, Madan K ; Peri, Irena ; Smirnoff, Patricia ; Birk, Yehudith ; Golan-Goldhirsh, Avi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a379t-5767f97867b7deca7fbc24694917e80ad35613ce87d59e5cb855c3f4dfe071fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Albumins - analysis</topic><topic>Albumins - metabolism</topic><topic>Amino Acids - analysis</topic><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>Biological and medical sciences</topic><topic>Chemical Fractionation</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endopeptidases - analysis</topic><topic>Endopeptidases - metabolism</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Globulins - analysis</topic><topic>Globulins - metabolism</topic><topic>Magnoliopsida - chemistry</topic><topic>Molecular Weight</topic><topic>Plant Extracts - chemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Proteins - pharmacology</topic><topic>Protease Inhibitors - analysis</topic><topic>Protease Inhibitors - pharmacology</topic><topic>Seeds - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shrestha, Madan K</creatorcontrib><creatorcontrib>Peri, Irena</creatorcontrib><creatorcontrib>Smirnoff, Patricia</creatorcontrib><creatorcontrib>Birk, Yehudith</creatorcontrib><creatorcontrib>Golan-Goldhirsh, Avi</creatorcontrib><collection>Istex</collection><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>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shrestha, Madan K</au><au>Peri, Irena</au><au>Smirnoff, Patricia</au><au>Birk, Yehudith</au><au>Golan-Goldhirsh, Avi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Jojoba Seed Meal Proteins Associated with Proteolytic and Protease Inhibitory Activities</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2002-09-25</date><risdate>2002</risdate><volume>50</volume><issue>20</issue><spage>5670</spage><epage>5675</epage><pages>5670-5675</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The jojoba, Simmondsia chinensis, is a characteristic desert plant native to the Sonoran desert. The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-inhibitory activity. SDS−PAGE showed two major proteins at 50 kDa and 25 kDa both in the albumins and in the globulins. The 25 kDa protein has trypsin- and chymotrypsin-inhibitory activities. In vitro digestibility of the globulins and albumins resembled that of casein and soybean protein concentrates and was increased after heat treatment. The increased digestibility achieved by boiling may be attributed to inactivation of the protease inhibitors and denaturation of proteins. Keywords: Jojoba meal protein; Simmondsia chinensis; solubility; protease inhibitory activity; digestibility</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12236696</pmid><doi>10.1021/jf020161h</doi><tpages>6</tpages></addata></record> |
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| subjects | Albumins - analysis Albumins - metabolism Amino Acids - analysis Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Biological and medical sciences Chemical Fractionation Electrophoresis, Polyacrylamide Gel Endopeptidases - analysis Endopeptidases - metabolism Food industries Fundamental and applied biological sciences. Psychology Globulins - analysis Globulins - metabolism Magnoliopsida - chemistry Molecular Weight Plant Extracts - chemistry Plant Proteins - chemistry Plant Proteins - metabolism Plant Proteins - pharmacology Protease Inhibitors - analysis Protease Inhibitors - pharmacology Seeds - chemistry |
| title | Jojoba Seed Meal Proteins Associated with Proteolytic and Protease Inhibitory Activities |
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