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Development of a greener flow-based analytical tool for the expeditious determination of total soluble proteins
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Orientador(es)
Resumo(s)
Protein hydrolysates are increasingly used in feed, underscoring the need for analytical tools for the rapid, reliable determination of total protein. This study revisited a merging-zones flow-based spectrophotometric method for minimizing reagent consumption and employs the Biuret reaction for the quantification of total soluble protein in by-products hydrolysates. The analytical method was optimized across different physical and chemical parameters such as: flowrate, reactor length, sample injection volume and reagents concentration. The use of different matrices relevant in the hydrolysis processes (acetate, phosphate, and hydrochloric acid) showed no significant interference (<10%) on the method's performance. Under optimal conditions, the method quantified hydrolysate protein within a dynamic range of 0.100–2.00 mg mL⁻¹ , with LOD and LOQ of 0.069 and 0.290 mg mL⁻¹ , respectively. Analyses of hydrolysates showed no significant differences compared with the reference method (<10%) while reducing analysis time from 30 min to 3 min per sample (triplicate). The method’s greenness, assessed by AGREE software, showed an improved score, from 0.58 to 0.76. The optimized protocol provides a fast, robust, and greener approach for monitoring protein hydrolysates in the food industry.
Descrição
Palavras-chave
Protein quantification Hydrolysates Biuret method Flow Injection Analysis Spectrophotometry
Contexto Educativo
Citação
Editora
Academic Press Inc.