NDLI: Purification and characterization of antioxidative peptides from round scad (Decapterus maruadsi) muscle protein hydrolysate.

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Purification and characterization of antioxidative peptides from round scad (Decapterus maruadsi) muscle protein hydrolysate.

Content Provider	Semantic Scholar
Author	Jiang, Haiping Tong, Tianzhe Sun, Jianhua Xu, Yuanjin Zhao, Zhongxing Liao, Dankui
Copyright Year	2014
Abstract	Muscle protein from round scad (Decapterus maruadsi) was hydrolyzed with five commercial proteases, namely, Alcalase, neutral protease, papain, pepsin, and trypsin. Round scad hydrolysate (RSH) prepared with Alcalase demonstrated high antioxidative activity. After ultrafiltration, RSH-III fraction (MW<5kDa) exhibited the strongest activity. Then, RSH-III was purified by gel filtration chromatography (Sephadex G-15) and separated into four fractions (A, B, C, and D), of which fraction B showed the highest antioxidative activity and was further purified using reverse-phase high-performance liquid chromatography twice. The purified peptides were identified as His-Asp-His-Pro-Val-Cys (706.8Da) and His-Glu-Lys-Val-Cys (614.7Da) by matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry. Subsequently, the identified peptides were synthesized, and their antioxidative activities were verified. Results indicated that the two novel peptides isolated from round scad muscle protein can be developed into antioxidative ingredients in functional foods.
File Format	PDF HTM / HTML
DOI	10.1016/j.foodchem.2013.12.074
PubMed reference number	24518328
Journal	Medline
Volume Number	154
Alternate Webpage(s)	http://ssu.ac.ir/cms/fileadmin/user_upload/Mtahghighat/tfood/asil-article/g-p2/Purification-and-characterization-of-antioxidative-peptides-from-round-scad-Decapterus-maruadsi-muscle-protein-hydrolysate_2014_Food-Chemistry.pdf
Alternate Webpage(s)	https://faculty.psau.edu.sa/filedownload/doc-3-pdf-d4ff76af57c1ebcc7eca3807b9a431a6-original.pdf
Journal	Food chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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