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Millettia speciosa is the dry root of the leguminous plant, which has the effect of tonifying the lung, strengthening the tendons and activating the collaterals. It is a famous dual-purpose plant for medicine and food in Lingnan area. In this paper, the research progress of the quality standard collection, variety identification, inspection, determination of effective ingredients and fingerprint quality evaluation of Millettia speciosa was reviewed. The advantages and disadvantages of the existing quality evaluation methods of Millettia speciosa were analyzed. The method of establishing the comprehensive quality evaluation system of Millettia speciosa was proposed, which can be used as a reference for the quality evaluation and quality control of Millettia speciosa. [ABSTRACT FROM AUTHOR]

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In order to lay the foundation for revealing the growth and development law and screening the genes related to root expansion by studying the biological activity of the amylase gene family of Millettia speciosa. Based on the transcriptome sequencing results of non-enlarged and enlarged root of M. speciosa, 28 daphnia magna amylase genes were screened by bioinformatics technology. The results showed that the molecular weights of amino acid sequences encoded by 28 amylase-related protein genes ranged from 20.78 to 349.39 KDa. They were all acidic proteins, some of the subcellular localization was in chloroplast. They had PLN02784 super family and AmyAc-family super family conserved domains. The proportion of random coil in the secondary structure was the largest excluded from MsAm1, MsAm7, MsAm8, MsAm15, MsAm16, MsAm22, MsAm23 and MsAm28. Tertiary structure prediction showed that the amylase of M. speciosa contained α-amylase structure, β-amylase structure, and isoamylase structure. Amylase gene family had 86 functional elements, and MsAm9 had the most functional elements(42). The phylogenetic tree showed that MsAm15, MsAm16 belonged to the same category and had motif 2, motif 3, motif 7, and MsAm4, MsAm24, MsAm26 belonged to the other same category. Compared to Arabidopsis thaliana anylase, AtBM4 and MsAm6, AtAM2 and MsAm2, AtBM8 and MsAm5, AtBM4 and MsAm6, AtAM10 and MsAm22, AtIM3 and MsAm17 belonged to the same category, respectively. These results could provide a theoretical basis for the further study of biological functions and regulation mechanism of 28 M. speciosa amylase, and provide a reference for the study of root enlargement and improvement of M. speciosa amylase varieties. [ABSTRACT FROM AUTHOR]