Harvesting microalgae presents a challenge in selecting the most economical method for low cost algal bioproducts. Previous studies have shown coagulation-flocculation to be the most efficient method for large scale microalgae harvesting. This study focused on modifying native potato starch with biogenic amines and optimizing the reaction parameters. Such modification rendered the starch cationic, with an ability to destabilize microalgae suspensions or colloids. The effect of time, temperature, and reactant concentrations on the zeta potential of the cationic amino starch was studied. Biogenic amines including putrescine, histamine, cadaverine, and tyramine were selected for study based on the number of nitrogen groups in their structure. Zeta potential for histamine cationic amino starch was significantly higher (+9.0±2.0 mV) at lower reaction temperatures, regardless of the amine to starch ratio and reaction time intervals. Putrescine, cadaverine, and tyramine cationic amino starches exhibited significantly higher zeta potential values (13.76±3.60, 6.81±1.64, and 5.68±1.60 mV, respectively) with amine to starch ratio higher than reaction stoichiometry, irrespective of reaction temperature or time intervals. This optimization study has presented a basis for designing reaction conditions for the synthesis of cationic amino starch from an inhomogeneous mix of biogenic amines derived from waste sources.
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http://dx.doi.org/10.1016/j.carbpol.2013.07.043 | DOI Listing |
ACS Phys Chem Au
January 2025
Instituto de Ciência e Tecnologia, Universidade Federal de São Paulo, São José dos Campos, 12247-014 São Paulo, Brazil.
The unique properties and versatile applications of natural deep eutectic solvents (NaDES) have sparked significant interest in the field of green chemistry. Comprised of natural components that form liquids at room temperature through strong noncovalent electrostatic interaction, these solvents are cost-effective, nontoxic, and versatile. Betaine chloride-based NaDES, in particular, have shown promise in biocatalysis and sugar extraction due to their excellent properties.
View Article and Find Full Text PDFACS Cent Sci
January 2025
The Second Affiliated Hospital of Zhejiang University School of Medicine, Life Sciences Institute, Zhejiang University, Hangzhou 310058, China.
Genetic encoding of noncanonical amino acids (ncAAs) with desired functionalities is an invaluable tool for the study of biological processes and the development of therapeutic drugs. However, existing ncAA incorporation strategies are rather time-consuming and have relatively low success rates. Here, we develop a virtual ncAA screener based on the analysis and modeling of the chemical properties of all reported ncAA substrates to virtually determine the recognition potential of candidate ncAAs.
View Article and Find Full Text PDFFront Mol Biosci
January 2025
Department of Biochemistry, Faculty of Agriculture, Zagazig University, Zagazig, Egypt.
Introduction: This study investigated the tryptic hydrolysis of β-lactoglobulin (BLG) for 30, 60, 90, and 120 min at 1/200 E/S (enzyme/substrate ratio, w/w) to prepare potentially anticarcinogenic peptides.
Methods: The properties of hydrolysates were characterized, including degree of hydrolysis, free amino acids, SDS-PAGE, FTIR, and antioxidant activity employing DPPH-assay, β-carotene/linoleic acid, and FRAP assay.
Results: BLG tryptic hydrolysate produced after 60 min hydrolysis recorded the highest antioxidant activity, and LCMS analysis revealed 162 peptides of molecular masses ranging from 800 to 5671Da, most of them are of hydrophobic nature.
ACS Omega
January 2025
Infectious Diseases Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu, Jammu and Kashmir 180001, India.
The insertion of β-amino acids and replacement of the amide bond with a urea bond in antimicrobial peptide sequences are promising approaches to enhance the antibacterial activity and improve proteolytic stability. Herein, we describe the synthesis, characterization, and antibacterial activity of short αβ cationic hybrid peptides LA-Orn-βAcc-PEA, ; LA-Lys-βAcc-PEA, ; and LA-Arg-βAcc-PEA, in which a C12 lipid chain is conjugated at the N terminus of peptide through urea bonds. Further, we evaluated all the peptides against both and methicillin-resistant (MRSA) and their multidrug resistant (MDR) clinical isolates.
View Article and Find Full Text PDFBiotechnol Prog
January 2025
Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
The production of disulfide-containing recombinant proteins often requires refolding of inclusion bodies before purification. A pre-refolding purification step is crucial for effective refolding because impurities in the inclusion bodies interfere with refolding and subsequent purification. This study presents a new pre-refolding procedure using a reversible S-cationization technique for protein solubilization and purification by reversed-phase high performance liquid chromatography.
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