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The isoelectric point (pI) is the pH of a solution at which the net charge of a protein becomes zero. In the present study, proteins present in the enzymatic extract (EE) of Canola Brassica napus L. obtained through solid-state fermentation (SSF) were dialyzed, and their isoelectric point (pI) was determined. Soluble protein (SP) and proteolytic activity (PA) were quantified in two extracts: replacement water (RW) and precipitated paste (PP) from the dialysis. Six pH levels were evaluated at two temperatures: 20 °C and 35 °C. The EE within the cellulose envelope was dialyzed for 72 h, with aliquots taken every 12 h. The results indicated that at 20 °C in RW, SP and PA were 0.1559 mg/g and 380.55 U/L at 60 h, respectively, while in PP at 35 °C, SP and PA were 0.279 mg/g and 772.20 U/L at 72 h, respectively. The pI was obtained at pH 4.0 with the maximum protein precipitation at 0.8445 mg/g. The increase in temperature raised the values of SP, PA, and favored the determination of the pI due to greater denaturation of the proteins.

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Determination of the Isoelectric Point of Proteins in Enzymatic Extract of Canola Waste Fermented with Yarrowia lipolytica

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  • 发表日期：

    2025年

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  • López-Trujillo Juan,
  • Hernández-Herrera José Antonio,
  • Charles-Rodríguez Ana Verónica,
  • Ortiz Cano Héctor Genaro,
  • Medina-Morales Miguel Ángel,
  • Tafolla-Arellano Julio César

摘要

The isoelectric point (pI) is the pH of a solution at which the net charge of a protein becomes zero. In the present study, proteins present in the enzymatic extract (EE) of Canola Brassica napus L. obtained through solid-state fermentation (SSF) were dialyzed, and their isoelectric point (pI) was determined. Soluble protein (SP) and proteolytic activity (PA) were quantified in two extracts: replacement water (RW) and precipitated paste (PP) from the dialysis. Six pH levels were evaluated at two temperatures: 20 °C and 35 °C. The EE within the cellulose envelope was dialyzed for 72 h, with aliquots taken every 12 h. The results indicated that at 20 °C in RW, SP and PA were 0.1559 mg/g and 380.55 U/L at 60 h, respectively, while in PP at 35 °C, SP and PA were 0.279 mg/g and 772.20 U/L at 72 h, respectively. The pI was obtained at pH 4.0 with the maximum protein precipitation at 0.8445 mg/g. The increase in temperature raised the values of SP, PA, and favored the determination of the pI due to greater denaturation of the proteins.