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1.
BioTech (Basel) ; 13(3)2024 Jun 24.
Artigo em Inglês | MEDLINE | ID: mdl-39051336

RESUMO

This work aimed to identify the influence of pH, molarity, w/v fraction, extraction time, agitation, and either a sodium (Na2HPO4·7H2O-NaH2PO4·H2O) or potassium buffer (K2HPO4-KH2PO4) used in the extraction of C-phycoerythrin (C-PE) from a thermotolerant strain of Potamosiphon sp. An experimental design (Minimum Run Resolution V Factorial Design) and a Central Composite Design (CCD) were used. According to the statistical results of the first design, the K-PO4 buffer, pH, molarity, and w/v fraction are vital factors that enhance the extractability of C-PE. The construction of a CCD design of the experiments suggests that the potassium phosphate buffer at pH 5.8, longer extraction times (50 min), and minimal extraction speed (1000 rpm) are ideal for maximizing C-PE concentration, while purity is unaffected by the design conditions. This optimization improves extraction yields and maintains the desired bright purple color of the phycobiliprotein.

2.
BioTech (Basel) ; 12(2)2023 Apr 23.
Artigo em Inglês | MEDLINE | ID: mdl-37218747

RESUMO

Drying the biomass produced is one of the critical steps to avoid cell degradation; however, its high energy cost is a significant technological barrier to improving this type of bioprocess's technical and economic feasibility. This work explores the impact of the biomass drying method of a strain of Potamosiphon sp. on the extraction efficiency of a phycoerythrin-rich protein extract. To achieve the above, the effect of time (12-24 h), temperature (40-70 °C), and drying method (convection oven and dehydrator) were determined using an I-best design with a response surface. According to the statistical results, the factors that most influence the extraction and purity of phycoerythrin are temperature and moisture removal by dehydration. The latter demonstrates that gentle drying of the biomass allows removing the most significant amount of moisture from the biomass without affecting the concentration or quality of temperature-sensitive proteins.

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