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Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates.

Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Research Abstract Details 

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  • Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Abstract Text:

    inge celusInge Celus,kristof brijsKristof Brijs,jan a delcourJan A Delcour,inge celusInge Celus,kristof brijsKristof Brijs,jan a delcourJan A Delcour,

    Brewers' spent grain (BSG) is the insoluble residue of barley malt resulting from the manufacture of wort. Although it is the main byproduct of the brewing industry, it has received little attention as a marketable commodity and is mainly used as animal feed. Our work focuses on one of the main constituents of BSG, i.e., the proteins. The lack of solubility of BSG proteins is one of the limitations for their more extensive use in food processing. We therefore aimed to generate BSG protein hydrolysates with improved technofunctional properties. BSG protein concentrate (BPC) was prepared by alkaline extraction of BSG and subsequent acid precipitation. BPC was enzymatically hydrolyzed in a pH-stat setup by several commercially available proteases (Alcalase, Flavourzyme, and Pepsin) for different times and/or with different enzyme concentrations in order to obtain hydrolysates with different degrees of hydrolysis (DH). Physicochemical properties, such as molecular weight (MW) distribution and hydrophobicity, as well as technofunctional properties, such as solubility, color, and emulsifying and foaming properties, were determined. Enzymatic hydrolysis of BPC improved emulsion and/or foam-forming properties. However, for the hydrolysates prepared with Alcalase and Pepsin, an increasing DH generally decreased emulsifying and foam-forming capacities. Moreover, the type of enzyme impacted the resulting technofunctional properties. Hydrolysates prepared with Flavourzyme showed good technofunctional properties, independent of the DH. Physicochemical characterization of the hydrolysates indicated the importance of protein fragments with relatively high MW (exceeding 14.5 k) and high surface hydrophobicity for favorable technofunctional properties.

    Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Publishing Authors By Initials

    i celusI Celus,k brijsK Brijs,ja delcourJA Delcour,i celusI Celus,k brijsK Brijs,ja delcourJA Delcour,

    For similar proteins: plant proteins research abstracts see: proteins: plant proteins research

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    Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of agricultural and food chemistry

    VOLUME: 55

    Page Numbers: 8703-10

    Journal Abbreviation: J. Agric. Food Chem.

    ISSN: 0021-8561

    DAY: 27

    MONTH: 09

    YEAR: 2007

    Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 374755

    Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Keywords Mesh Terms:

    KEYWORDS: Plant Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates. Information

    Substance Name: Peptide Hydrolases

    Registry Number: EC 3.4.-

    Grant and Affiliation Information for Enzymatic hydrolysis of brewers' spent grain proteins and technofunctional properties of the resulting hydrolysates.

    AFFILIATION: Laboratory of Food Chemistry and Biochemistry, Katholieke Universiteit Leuven, Kasteelpark Arenberg 20, B-3001 Leuven, Belgium. inge.celus@biw.kuleuven.be

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Agric Food Chem

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