Babu Neelu Suresh, Halami Prakash Motiram, Kudre Tanaji Ganptgonda
Department of Meat and Marine Sciences, CSIR-Central Food Technological Research Institute, Mysuru, India.
Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India.
J Sci Food Agric. 2025 Jul 11. doi: 10.1002/jsfa.70042.
Fish proteins are considered as noteworthy sources of bioactive peptides and their preparation using Lactobacillus fermentation has gained more importance because of health benefits. The present research focuses on the production, purification and identification of novel antioxidant peptides from fermented Piaractus brachypomus meat protein hydrolysate (PBMPH) using Pediococcus pentosaceus.
The PBMPH was produced using a 300 g L P. brachypomus meat concentration, 20 g L sucrose and 48 h of fermentation. Antioxidant peptides were separated from PBMPH using ultrafiltration (3 kDa molecular weight cutoff), Sephadex G-25 gel filtration chromatography, and reverse-phase HPLC, respectively. Ultrafiltration demonstrated that PBMPH-UF-1 fraction (molecular weight < 3 kDa) exhibited notably higher ferric-reducing antioxidant power (FRAP), 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) radical scavenging and Fe chelating activity (P < 0.05) than PBMPH-UF-2 fraction (molecular weight > 3 kDa). Subsequently, the separation of PBMPH-UF-1 peptide fraction by Sephadex G-25 resulted in three fractions of antioxidant peptides. Amid these peptide fractions, PBMPH-GF-1 revealed significantly higher antioxidant activities (FRAP, DPPH, ABTS and Fe chelating activity) (P < 0.05). Furthermore, the PBMPH-GF-1 peptide fraction was subjected to reverse-phase HPLC, in which eight peptide fractions were obtained. PBMPH-RPH-7 peptide fraction had the highest antioxidant activities than other fraction counterparts. Liquid chromatography-tandem mass spectrometry further identified the peptide sequence of the PBMPH-RPH-7 fraction and unveiled two antioxidant peptides, namely LTDIESM (749.36 Da) and DPGYMHHKFAIV (1429.68 Da), with amino acid sequences Leu-Thr-Asp-Ile-Glu-Ser-Met and Asp-Pro-Gly-Tyr-Met-His-His-Lys-Phe-Ala-Ile-Val, respectively.
The findings of the present study emphasize the production and purification of novel antioxidant peptides from P. brachypomus meat protein through P. pentosaceus fermentation, which can be utilized as a potential antioxidant in functional foods and nutraceutical products. © 2025 Society of Chemical Industry.
鱼蛋白被认为是生物活性肽的重要来源，由于其对健康有益，利用乳酸杆菌发酵制备鱼蛋白受到了更多关注。本研究聚焦于利用戊糖片球菌从发酵的短盖巨脂鲤肉蛋白水解物（PBMPH）中生产、纯化和鉴定新型抗氧化肽。
使用300 g/L的短盖巨脂鲤肉浓度、20 g/L蔗糖并发酵48小时来生产PBMPH。分别采用超滤（截留分子量3 kDa）、Sephadex G - 25凝胶过滤色谱和反相高效液相色谱从PBMPH中分离抗氧化肽。超滤结果表明，PBMPH - UF - 1组分（分子量 < 3 kDa）的铁还原抗氧化能力（FRAP）、2,2 - 二苯基 - 1 - 苦基肼自由基（DPPH）清除能力、2,2'- 偶氮 - 双（3 - 乙基苯并噻唑啉 - 6 - 磺酸）二铵盐（ABTS）自由基清除能力和铁螯合活性显著高于PBMPH - UF - 2组分（分子量 > 3 kDa）（P < 0.05）。随后，通过Sephadex G - 25对PBMPH - UF - 1肽组分进行分离，得到了三个抗氧化肽组分。在这些肽组分中，PBMPH - GF - 1显示出显著更高的抗氧化活性（FRAP、DPPH、ABTS和铁螯合活性）（P < 0.05）。此外，对PBMPH - GF - 1肽组分进行反相高效液相色谱分析，得到了八个肽组分。PBMPH - RPH - 7肽组分的抗氧化活性高于其他组分。液相色谱 - 串联质谱进一步鉴定了PBMPH - RPH - 7组分的肽序列，并揭示了两种抗氧化肽，即LTDIESM（749.36 Da）和DPGYMHHKFAIV（1429.68 Da），其氨基酸序列分别为Leu - Thr - Asp - Ile - Glu - Ser - Met和Asp - Pro - Gly - Tyr - Met - His - His - Lys - Phe - Ala - Ile - Val。
本研究结果强调了通过戊糖片球菌发酵从短盖巨脂鲤肉蛋白中生产和纯化新型抗氧化肽，这些肽可作为功能性食品和营养保健品中的潜在抗氧化剂。© 2025化学工业协会
