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dc.contributor.advisorPrice, Ralph L.en_US
dc.contributor.authorCardoso, Fernando Antonioen_US
dc.creatorCardoso, Fernando Antonioen_US
dc.date.accessioned2013-04-18T10:01:51Zen
dc.date.available2013-04-18T10:01:51Zen
dc.date.issued1980en_US
dc.identifier.urihttp://hdl.handle.net/10150/282747en
dc.description.abstractTwo defatted jojoba seed meals were prepared; one using whole seeds (JM), and the other from which seed coats were removed prior to extraction of the oil (DJM). The protein content of both meals was about 24%. The proteins from JM and DJM were extracted according to their solubility in water, dilute saline, alcohol, and alkali solutions. These extractions produced the albumin, globulin, prolamine and glutelin protein concentrates. The major concentration of proteins in jojoba were the albumin (65%) and globulin (21%) fractions. The amino acid compositions of both JM and DJM were found to be very similar. Methionine was the limiting amino acid in jojoba seed proteins. The protein composition was determined, and the molecular weight was estimated through chromatographic analysis using gel filtration on Sephadex G-100 and ion-exchange chromatography on DEAE-Sephadex and CM-Sephadex. At least 5 separate protein fractions in each of the albumin and globulin concentrates and 8 separate protein fractions in each of the prolamine and glutelin concentrates were found. The molecular weights of jojoba protein concentrates varied from 19,000 to 150,000 for albumins, from 18,000 to 128,800 for globulins, from 11,700 to 141,200 for prolamines, and from 29,500 to 150,000 for glutelins. All protein concentrates showed very good fat absorption and solubility at values of pH below 3.0 and above 4.0. Albumins and globulins showed very good foamability and emulsion properties. The prolamine and glutelin concentrates showed very poor foamability and emulsion properties. The buffering capacity of jojoba protein concentrates was very low.
dc.language.isoen_USen_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.subjectJojoba -- Sonoran Desert.en_US
dc.subjectProteins.en_US
dc.subjectJojoba -- Analysis.en_US
dc.titleEXTRACTION, CHARACTERIZATION AND FUNCTIONAL PROPERTIES OF JOJOBA PROTEINSen_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.identifier.oclc7518910en_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.leveldoctoralen_US
dc.identifier.proquest8104291en_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineAgricultural Biochemistry and Nutritionen_US
thesis.degree.namePh.D.en_US
dc.identifier.bibrecord.b13415864en_US
refterms.dateFOA2018-08-28T10:10:34Z
html.description.abstractTwo defatted jojoba seed meals were prepared; one using whole seeds (JM), and the other from which seed coats were removed prior to extraction of the oil (DJM). The protein content of both meals was about 24%. The proteins from JM and DJM were extracted according to their solubility in water, dilute saline, alcohol, and alkali solutions. These extractions produced the albumin, globulin, prolamine and glutelin protein concentrates. The major concentration of proteins in jojoba were the albumin (65%) and globulin (21%) fractions. The amino acid compositions of both JM and DJM were found to be very similar. Methionine was the limiting amino acid in jojoba seed proteins. The protein composition was determined, and the molecular weight was estimated through chromatographic analysis using gel filtration on Sephadex G-100 and ion-exchange chromatography on DEAE-Sephadex and CM-Sephadex. At least 5 separate protein fractions in each of the albumin and globulin concentrates and 8 separate protein fractions in each of the prolamine and glutelin concentrates were found. The molecular weights of jojoba protein concentrates varied from 19,000 to 150,000 for albumins, from 18,000 to 128,800 for globulins, from 11,700 to 141,200 for prolamines, and from 29,500 to 150,000 for glutelins. All protein concentrates showed very good fat absorption and solubility at values of pH below 3.0 and above 4.0. Albumins and globulins showed very good foamability and emulsion properties. The prolamine and glutelin concentrates showed very poor foamability and emulsion properties. The buffering capacity of jojoba protein concentrates was very low.


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