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February 19, 2026Journal of King Saud University - Science0 citationsOpen Access

Characterization of protein extracted from the Omani seaweed- Hypnea bryoides

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HAHala Hilal Al-MawaliAAAhmed Ali Musalem Al-Alawi

Key Points

  • The aim is to extract protein from Hypnea bryoides and assess its functional and chemical properties.
  • Extracted protein using 0.3 M NaOH at pH 12.
  • Measured yield (31%) and purity (88.50 ± 0.71%).
  • Evaluated oil-holding and water-holding capacities, foaming capacity, solubility, and emulsifying stability at various pH levels.
  • Assessed in vitro digestibility (62.62 ± 3.29%).
  • Conducted molecular analysis to assess secondary structures.
  • Protein exhibited higher oil-holding capacity (13.56 ± 0.26 g oil/g protein) than water-holding capacity (9.61 ± 0.15 g water/g protein).
  • The highest foaming stability was found at pH 4, while emulsifying capacity peaked at pH 8 and 10.
  • β-sheet structures were identified as the primary secondary structural component of the protein.
  • Essential amino acids represented 35.08% of the total profile, with methionine + cysteine identified as limiting.

Abstract

Hypnea bryoides ( H. bryoides ), a species of red seaweed (Rhodophyta), was previously found to contain a significant amount of protein. This study aimed to extract protein from H. bryoides and examine its functional and chemical properties, thereby facilitating its use. The protein was extracted in an alkaline solution (0.3 M NaOH, pH 12). The extraction yielded 31% from the original existing quantity, and the purity was 88.50 ± 0.71%. The protein demonstrated a higher oil-holding capacity (13.56 ± 0.26 g oil/g protein) compared to its water-holding capacity (9.61 ± 0.15 g water/g protein). The highest foaming capacity, solubility, emulsifying capacity, and stability were observed at pH 8 and 10 ( p ≤0.05), while the most outstanding foaming stability occurred at pH 4. The in vitro digestibility was 62.62 ± 3.29%. Furthermore, the molecular analysis revealed that β-sheet structures constitute the primary secondary structural component of H. bryoides proteins. A broad range of protein molecules with varying molecular weights (0.4-125.2 kDa) was identified. The amino acid profile indicated that essential amino acids accounted for 35.08% of the total, with methionine + cysteine as the limiting amino acid. Overall, this seaweed protein demonstrated good functional and chemical properties, making it suitable for many food applications.

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Cite This Study

Al-Mawali et al. (2026) studied this question.

synapsesocial.com/papers/6996a8c7ecb39a600b3efe58https://doi.org/10.25259/jksus_1044_2025
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