Composition and Molecular Weight Distribution of Carob Germ Protein Fractions

Biochemical properties of carob germ proteins were analyzed using a combination of selective extraction, reversed-phase high-performance liquid chromatography (RP-HPLC), size exclusion chromatography (SEC) coupled with multiangle laser light scattering (SEC-MALS), and electrophoretic analysis. Using...

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Bibliographic Details
Published inJournal of agricultural and food chemistry Vol. 58; no. 13; pp. 7794 - 7800
Main Authors Smith, Brennan M, Bean, Scott R, Schober, Tilman J, Tilley, Michael, Herald, Thomas J, Aramouni, Fadi
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 14.07.2010
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Summary:Biochemical properties of carob germ proteins were analyzed using a combination of selective extraction, reversed-phase high-performance liquid chromatography (RP-HPLC), size exclusion chromatography (SEC) coupled with multiangle laser light scattering (SEC-MALS), and electrophoretic analysis. Using a modified Osborne extraction procedure, carob germ flour proteins were found to contain ∼32% albumin and globulin and ∼68% glutelin with no prolamins detected. The albumin and globulin fraction was found to contain low amounts of disulfide-bonded polymers with relatively low M w ranging up to 5 × 106 Da. The glutelin fraction, however, was found to contain large amounts of high molecular weight disulfide-bonded polymers with M w up to 8 × 107 Da. When extracted under nonreducing conditions and divided into soluble and insoluble proteins as typically done for wheat gluten, carob germ proteins were found to be almost entirely (∼95%) in the soluble fraction with only (∼5%) in the insoluble fraction. As in wheat, SEC-MALS analysis showed that the insoluble proteins had a greater M w than the soluble proteins and ranged up to 8 × 107 Da. The lower M w distribution of the polymeric proteins of carob germ flour may account for differences in functionality between wheat and carob germ flour.
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ISSN:0021-8561
1520-5118
DOI:10.1021/jf101523p