Evaluation of genetic diversity in Korean soybean landraces by protein banding patterns using high-throughput screening
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J. Crop Sci. Biotech. 2013 (Sep) 16 (3) : 189~207 DOI No. 10.1007/s12892-013-0068-8 RESEARCH ARTICLE
Evaluation of Genetic Diversity in Korean Soybean Landraces by Protein Banding Patterns Using High-Throughput Screening Vijayanand Velusamy, Kyung Jun Lee, Bo-Keun Ha, Jin-Baek Kim, Sang Hoon Kim, Joon-Woo Ahn, Si-Yong Kang, Dong Sub Kim* Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 1266 Sinjeong, Jeongeup, Jeonbuk, 580-185, Korea Received: June 03, 2013 / Revised: August 19, 2013 / Accepted: September 12, 2013 Ⓒ Korean Society of Crop Science and Springer 2013
Abstract The agronomic performance and storage protein patterns of 722 soybean landraces collected from eight geographically different Korean locations were investigated. The days to 50% flowering, days to maturity, and 100-seed weight ranged from 68.9 to 71.9 (d), 140.1 to 146.6 (d), and 22.4 to 26.8 (g), respectively. High-throughput protein profiling electrophoresis was performed, and the banding patterns were analyzed. Among the 722 soybean landraces, lipoxygenase bands were found to be absent in 21 lines. Nei’s gene diversity (h) ranged from 0 to 0.2642, with an average value of 0.1565. The mean coefficient of gene differentiation (Gst) was 0.0944, and the estimated gene flow (Nm) in the population was 4.7971. In a correlation matrix between the agronomic traits and protein banding patterns, the acidic banding pattern was significantly associated with all the other factors. The phenotypic and genotypic differences of the collection areas were evaluated, and the excellent soybean lines with high-value proteins, including 11S globulins, or without antinutritional factors such as lipoxygenase and trypsin inhibitor were selected. Key words: antinutritional factors, protein profiling electrophoresis, protein sub-units, seed storage protein, soybean diversity
Introduction Soybean (Glycine max L.) storage proteins have two major fractions, β-conglycinin (7S) and glycinin (11S), accounting for more than 70% of the total protein (Tsukada et al. 1986), and their contents have been shown to vary among soybean varieties and environmental conditions (Hughes and Murphy 1983; Murphy and Resurreccion 1984; Saio et al. 1969; Wolf et al. 1961). The protein extracts from different soybean cultivars exhibit unique amounts of clear and indistinct banding patterns (Liu et al. 2007). Wolf and colleagues (Wolf and Briggs 1956; Wolf and Tamura 1968) first classified soy proteins into 2S, 7S, 11S, and 15S components based on a classical ultracentrifuge method and later estimated that 2S, 7S, 11S, and 15S accounted for 22, 37, 31, Dong Sub Kim ( ) E-mail: [email protected] Tel: +82-63-570-3311 / Fax +82-63-570-3319 First two authors equally contributed. The Korean Society of Crop Science
and 11%, respectively, of the total protein in soybeans. Soy protein is a major protein source in the food industry (Liu et al. 2007), and the 11S and 7S components have been found to have significantly different physical–chemical and functional propertie
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