Molecular and spectroscopic characterisation of a low molecular weight seed storage protein from yellow mustard (Sinapis alba L.) |
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| Institution: | 1. School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China;2. College of Food Science, South China Agricultural University, Guangzhou 510640, China;3. Research Institute for Food Nutrition and Human Health, Guangzhou, China;1. U.S. Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, 600 East Mermaid Lane, Wyndmoor, PA 19038, United States;2. Jiangnan University, 1800 Lihu Ave., Wuxi, Jiangsu 214122, China |
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| Abstract: | - 1.1. A 1.7S protein has been purified from mustard seeds (Sinapis alba L.). This protein, soluble in water and dilute salt solutions, is considered as an albumin and constitutes about 10% of the total soluble protein in mustard seeds.
- 2.2. Its molecular weight is approximately 15,000 and is composed of two polypeptide chains (Mr = 9500 and 5000), linked by two disulfide bridges.
- 3.3. The amino acid compositions of both subunits as well as of the native protein are reported, showing a strong homology with napins from Brassica napus L.
- 4.4. The ultraviolet absorption, fluorescence emission and circular dichroism spectra of the purified protein have been obtained. The mustard protein exhibits about 50% α-helix with a very low β-structure content. Based on its structural characteristics, a zein-like packing is proposed for this protein from mustard seeds.
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