Please use this identifier to cite or link to this item: http://localhost:80/xmlui/handle/123456789/14625
Title: Preparation and antioxidant properties of crayfish (Procambarus clarkii) By-products protein hydrolysates and ultra filtration fractions
Authors: Tang, Zhihong
Yu, Liang
Wen, Shaohong
Zhang, Kaiqi
Sun, Yongrong
Lv, Jiasen
Ju, Bao
Hu, d Zhongliang
Keywords: Crayfish by-products
hydrolysis
ultrafiltration
antioxidant activity
Issue Date: 20-Sep-2019
Publisher: Karachi:Pakistan Journal of Pharmaceutical Sciences, university of Karachi.
Citation: Tang, Z., Yu, L., Wen, S., Zhang, K., Sun, Y., Lv, J., ... & Hu, Z. (2019). Preparation and antioxidant properties of crayfish (Procambarus Clarkii) By-products protein hydrolysates and ultra filtration fractions. Pakistan Journal of Pharmaceutical Sciences, 32(SI5), 2391-2398.
Abstract: Protein isolate from crayfish by-products (CBPI) were hydrolyzed using Alcalase, neutrase, pancreatin and bromelain. Hydrolysis by Alcalase had more remarkable digesting efficiency on crayfish by-products protein than that by the other enzymes. Therefore, protein hydrolysate from Alcalase digestion (CBPHa) was selected to be fractionated by ultrafiltration according to molecular weight into three fractions F1 (MW <1kDa), F2 (MW 1-3kDa) and F3 (MW 310kDa). The amino acid determination revealed that CBPI had essential amino acid (EAA) close to that required for human protein synthesis. In vitro activity experiments showed that CBPHa and its fractions possessed considerable antioxidant activity. F1 exhibited the highest DPPH, superoxide radicals scavenging activities and Fe2+ chelating ability, whereas F2 showed the best hydroxyl radicals scavenging capacity and reducing power. In addition, all the fractions showed higher super oxide radical scavenging activity than the crude hydrolysates. Our findings suggest that CBPHa and their ultra filtration fractions have the potential for use in nutraceutical and functional food industries to maximize the use of crayfish processing by-products.
URI: http://142.54.178.187:9060/xmlui/handle/123456789/14625
ISSN: 1011-601X
Appears in Collections:Issue 5 (Special)

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