Literature DB >> 30811185

Chemical Lipophilization of Bovine α-Lactalbumin with Saturated Fatty Acyl Residues: Effect on Structure and Functional Properties.

Liliana G Mendoza-Sánchez1, Maribel Jiménez-Fernández2, Guiomar Melgar-Lalanne2, Gustavo F Gutiérrez-López1, Andrés Hernández-Arana3, Francisco Reyes-Espinosa3, Humberto Hernández-Sánchez1.   

Abstract

Bovine α-lactalbumin (α-LA) was chemically modified by the covalent attachment of fatty acid residues of different length (lauroyl, palmitoyl, and stearoyl) to modify its functional and antioxidant properties. Structural changes, functional properties, and antioxidant capacity in the pH interval between 3 and 10 were analyzed. Surface properties were improved. The esterification increased the hydrophobic interactions leading to a reduction in the solubility dependent on the incorporation ratio of the fatty acid residues. Improvement in emulsifying, foaming, and antioxidant properties were observed when the length of the fatty acid chains was short and mostly at a basic pH. With these results in mind, experiments could be conducted for the technological applications of these derivatives in the food, pharmaceutical, and cosmetic industries.

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Keywords:  antioxidant activity; functional properties; lipophilization; structural analysis; α-lactalbumin

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Year:  2019        PMID: 30811185     DOI: 10.1021/acs.jafc.8b05174

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  1 in total

1.  Functional Properties of Rye Prolamin (Secalin) and Their Improvement by Protein Lipophilization through Capric Acid Covalent Binding.

Authors:  Zeinab Qazanfarzadeh; Mahdi Kadivar; Hajar Shekarchizadeh; Raffaele Porta
Journal:  Foods       Date:  2021-03-01
  1 in total

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