Scholarlink

<p>Zein, an intact corn protein, possesses high functional value. Its poor solubility and complex protein structure in native form restrict its applicability in food systems. However, limited information on systematic comparisons of enzyme-specific hydrolysis and hydrolysis time is available. Therefore, the objective of current study was to evaluate functional characteristics of zein via controlled proteolytic hydrolysis by using Papain, Flavourzyme and Alcalase at 1:50 enzyme-substrate ratio, followed by hydrolysate sampling at 60th, 120th and 180th minutes of hydrolysis. The resultant zein hydrolysates were analyzed for SDS-PAGE, FTIR, Degree of Hydrolysis (DH %), anti-oxidant activity (DPPH assay) and amino acid profiling. SDS-PAGE analysis revealed that Alcalase generated lower molecular weight peptides (10–20 KDa) whereas Papain (45–55 KDa) and Flavourzyme (25–35 KDa) generated relatively larger peptides. FTIR spectroscopy showed progressive structural changes, indicating greater peptide bond cleavage and secondary structure changes during Alcalase hydrolysis. The degree of hydrolysis was highest in Alcalase-180 (39.33%), followed by Alcalase-120 (36.33%) and Alcalase-60 (31.33%). Antioxidant activity assays demonstrated that hydrolysates, particularly those from Alcalase-180, exhibited enhanced radical scavenging potential (60%) followed by Flavourzyme-180 (56%) and Alcalase-120 (53%). Similarly, amino acid analysis confirmed significantly higher levels (<i>p</i> &lt; 0.05) of hydrophobic amino acids in hydrolysates generated by zein treated with Alcalase for 180&#xa0;min. Overall, the results suggest that enzymatic hydrolysis, particularly using Alcalse for 180&#xa0;min, improves functional characteristics of zein.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Proteolytic hydrolysis and functional characterization of zein protein hydrolysates

  • 期刊论文

  • 发表日期：

    2026年4月28日

查看全文
  • Misbah Sharif,
  • Ambreen Naz,
  • Umar Farooq,
  • Kashif Razzaq

摘要

Zein, an intact corn protein, possesses high functional value. Its poor solubility and complex protein structure in native form restrict its applicability in food systems. However, limited information on systematic comparisons of enzyme-specific hydrolysis and hydrolysis time is available. Therefore, the objective of current study was to evaluate functional characteristics of zein via controlled proteolytic hydrolysis by using Papain, Flavourzyme and Alcalase at 1:50 enzyme-substrate ratio, followed by hydrolysate sampling at 60th, 120th and 180th minutes of hydrolysis. The resultant zein hydrolysates were analyzed for SDS-PAGE, FTIR, Degree of Hydrolysis (DH %), anti-oxidant activity (DPPH assay) and amino acid profiling. SDS-PAGE analysis revealed that Alcalase generated lower molecular weight peptides (10–20 KDa) whereas Papain (45–55 KDa) and Flavourzyme (25–35 KDa) generated relatively larger peptides. FTIR spectroscopy showed progressive structural changes, indicating greater peptide bond cleavage and secondary structure changes during Alcalase hydrolysis. The degree of hydrolysis was highest in Alcalase-180 (39.33%), followed by Alcalase-120 (36.33%) and Alcalase-60 (31.33%). Antioxidant activity assays demonstrated that hydrolysates, particularly those from Alcalase-180, exhibited enhanced radical scavenging potential (60%) followed by Flavourzyme-180 (56%) and Alcalase-120 (53%). Similarly, amino acid analysis confirmed significantly higher levels (p < 0.05) of hydrophobic amino acids in hydrolysates generated by zein treated with Alcalase for 180 min. Overall, the results suggest that enzymatic hydrolysis, particularly using Alcalse for 180 min, improves functional characteristics of zein.