Location: Location not imported yet.Title: Influence of methylation on the effectiveness of meat and bone meal protein as a bioflocculant
|ESSANDOH, MATTHEW - Oak Ridge Institute For Science And Education (ORISE)|
|NEIMAN, CHRISTINE - Oak Ridge Institute For Science And Education (ORISE)|
Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/26/2020
Publication Date: 4/28/2020
Citation: Essandoh, M., Garcia, R.A., Neiman, C., Strahan, G.D. 2020. Influence of methylation on the effectiveness of meat and bone meal protein as a bioflocculant. Journal of Agricultural and Food Chemistry. 122:55-61. https://doi.org/10.1016/j.fbp.2020.03.009.
Interpretive Summary: Meat and bone meal protein is a product from rendering industry. Unfortunately, the utilization of MBM protein is very difficult because it has poor solubility and very heterogeneous in nature. We have previously shown that we can reduce the negative charges on proteins and use it as an effective flocculant. In this study, we combined both acid hydrolysis (to improve MBM solubility) and methylation to generate a new bioflocculant. The performance of the resulting product was tested. The methylated MBM protein was shown to be effective in clarifying a colloidal or cloudy suspension compared to using MBM protein alone. These results are very important considering the fact that commercial synthetic flocculants have a lot of environmental issues.
Technical Abstract: Efficient utilization of products from the rendering industry is highly desirable from economical and environmental viewpoints. In this study, the enhancement in the application of meat and bone meal (MBM) protein as a bioflocculant was studied through methylation and dilute acid hydrolysis. The methylated reaction was performed under acidic methanol at 25 oC and 48 h using an MBM concentration of 3 g/L. Both raw MBM and methylated MBM (MeMBM) samples were subject to dilute acid hydrolysis for 2 h at 105 oC. The crude protein content of MBM and MeMBM after dilute acid hydrolysis were found to be 42.8% and 64.9%, respectively. Nuclear magnetic resonance (HSQC and CIGAR-HMBC) revealed that MBM proteins are being effectively methylated at their carboxylic acid groups. Size exclusion chromatography (SEC) coupled with UV-MALS-IV-dRI detection system were used to obtained information about the hydrolyzed MBM and MeMBM. The MeMBM protein hydrolysate (peak KCE = 2.4) showed enhanced flocculant properties compared to the raw MBM hydrolysate (peak KCE = 1.8) at all studied experimental conditions: flocculant dose, settling time, and suspension pH. The study revealed how methylation when used in combination with dilute acid hydrolysis can successfully improve the flocculation ability of an economical rendered animal protein.