Purification and characterisation of antioxidant and nitric oxide inhibitory peptides from Tilapia (Oreochromis niloticus) protein hydrolysate |
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| Authors: | Sureeporn Kangsanant Chakree Thongraung Chaweewan Jansakul Michael Murkovic Vatcharee Seechamnanturakit |
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| Affiliation: | 1. Nutraceutical and Functional Food Research and Development Center, Faculty of Agro‐Industry, Prince of Songkla University, Hat Yai, Songkhla, Thailand;2. Department of Food Technology, Faculty of Agro‐Industry, Prince of Songkla University, Hat Yai, Songkhla, Thailand;3. Department of Thai Medicine, Faculty of Traditional Thai Medicine, Prince of Songkla University, Hat Yai, Songkhla, Thailand;4. Institute of Biochemistry, Graz University of Technology, Graz, Austria |
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| Abstract: | Nitric oxide (NO)‐inhibitory and antioxidative activities of tilapia hydrolysates were prepared using ultrasound pretreatment at 70 W for 30 and 45 min, respectively, followed by Flavourzyme hydrolysis for 1 h. Both hydrolysates were fractionated using size exclusion chromatography on Sephadex G‐25 column and purified by RP‐HPLC. The amino acid sequence of the most potent and purified fractions was determined using LC/MS/MS. The antioxidant peptide (KAFAVIDQDKSGFIEEDELKLFLQNFSAGARAGDSDGDGKIGVDEFAALVK, MW: 6334.49 KDa) and NO‐inhibitory peptide (AFAVIDQDKSGFIEEDELKLFLQNFSAGARAGDSDGDGKIGVDEFAALVK, MW: 6309.49 Da) produced no cytotoxicity in RAW264.7 macrophage cell lines at the concentration of 100 mg mL?1. The purified peptides at the concentration 100 μg mL?1 possessed antioxidative and NO‐inhibitory activities 83.0 ± 1.1% and 40.9 ± 0.2%, respectively, which were about 100 times those of their counterpart crude hydrolysates. |
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| Keywords: | Amino acid sequence antioxidative activity nitric oxide inhibitory activity purification tilapia hydrolysate |
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