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      Ultrasound-assisted alkali removal of proteins from wastewater generated during oil bodies extraction

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          Abstract

          In this study, an ultrasonic-assisted alkaline method was used to remove proteins from wastewater generated during oil-body extraction, and the effects of different ultrasonic power settings (0, 150, 300, and 450 W) on protein recovery were investigated. The recoveries of the ultrasonically treated samples were higher than those of the samples without ultrasonic treatment, and the protein recoveries increased with increasing power, with a protein recovery of 50.10 % ± 0.19 % when the ultrasonic power was 450 W. Amino acid analysis showed that the amino acids comprising the recovered samples were consistent, regardless of the ultrasonic power used, but significant differences in the contents of amino acids were observed. No significant changes were observed in the protein electrophoretic profile using dodecyl polyacrylamide gel, indicating that sonication did not change the primary structures of the recovered samples. Fourier transform infrared and fluorescence spectroscopy revealed that the molecular structures of the samples changed after sonication, and the fluorescence intensity increased gradually with increasing sonication power. The contents of α-helices and random coils obtained at an ultrasonic power of 450 W decreased to 13.44 % and 14.31 %, respectively, whereas the β-sheet content generally increased. The denaturation temperatures of the proteins were determined using differential scanning calorimetry, and ultrasound treatment reduced the denaturation temperatures of the samples, which was associated with the structural and conformational changes caused by their chemical bonding. The solubility of the recovered protein increased with increasing ultrasound power, and a high solubility was essential in good emulsification. The emulsification of the samples was improved well. In conclusion, ultrasound treatment changed the structure and thus improved the functional properties of the protein.

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          Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions

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            Effects of ultrasound on the structure and physical properties of black bean protein isolates

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              Structural and functional changes in ultrasonicated bovine serum albumin solutions.

              Effects of high-intensity ultrasonication on functional and structural properties of aqueous bovine serum albumin (BSA) solutions were investigated. The functional properties of BSA were altered by ultrasonication. Surface activity of BSA increased. Minimal changes were observed in the global structure of BSA but surface charge increased particularly at basic pH values (e.g. pH>9). While dynamic light scattering measurements indicated that the particle size increased up to 3.4 times after 90 min of sonication, no significant increase in the oligomeric state of BSA using blue native PAGE was observed. The amount of free sulfhydryl groups in BSA after 90 min of sonication decreased. The increased particle size and decreased number of free sylfhydryl groups may be attributed to formation of protein aggregates. Surface hydrophobicity increased and circular dichroism spectroscopy and FTIR analysis indicated changes in the secondary structure of BSA. We hypothesize that mechanical, thermal and chemical effects of ultrasonication resulted in structural changes in BSA that altered the functional properties of the macromolecule which may be attributed to the formation of an ultrasonically induced state that differs from a thermally, mechanically or solvent induced state.
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                Author and article information

                Contributors
                Journal
                Ultrason Sonochem
                Ultrason Sonochem
                Ultrasonics Sonochemistry
                Elsevier
                1350-4177
                1873-2828
                08 May 2023
                June 2023
                08 May 2023
                : 96
                : 106436
                Affiliations
                [a ]College of Food Science, Northeast Agricultural University, Harbin 150030, China
                [b ]Heilongjiang Open University, Harbin, Heilongjiang 150030, China
                Author notes
                Article
                S1350-4177(23)00148-7 106436
                10.1016/j.ultsonch.2023.106436
                10352604
                30d5eeb1-5548-42b4-8e8d-cd59f688d204
                © 2023 The Authors. Published by Elsevier B.V.

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                : 9 December 2022
                : 24 April 2023
                : 4 May 2023
                Categories
                Ultrasonic Degradation of Pollutant

                wastewater,protein,ultrasound-assisted alkali method,structural property,functional property

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