A glycosidic germacradienolide from Eupatorium altissimum

The isolation and structure determination of a glycosidic germacradienolide from Eupatorium altissimum are reported. Eupatorin and 5-hydroxy-3′,4′,6,7-tetramethoxyflavone were also found.     

Chemical constituents from Saussurea licentiana Hand.-Mazz

Chemical investigation of Saussurea licentiana led to the isolation of ten compounds, and their structures were identified to be dia-aurantiamide acetate (1), (+)-pinoresinol 4-O-β-D-glucoside (2), encelin (3), apigenin (4), luteolin (5), jaceosidin (6), luteolin -7-O-β-D- glucopyranoside (7), α-amyrin (8), β-amyrin (9), taraxasterol (10) on the basis of mass and NMR spectra. This is the first report on the occurrence of compounds 1, and 2 in the genus Saussurea while 1 is reported for the first time from Asteraceae. This work also represents the first phytochemical work on the whole plants of S. licentiana.     

Proacaciberin,A cyanogenic glycoside from Acacia sieberiana var. Woodii

A new cyanogenic glycoside isolated from pods of Acacia sieberiana var. woodii has been shown by chemical and spectroscopic methods to be (2S)-2-[(6-O-α-l-arabinopyranosyl-β-d-glucopyranosyl)oxy]-3-methylbut-3-enenitrileo. Acid-catalysed hydrolysis of the glycoside afforded arabinose and proacacipetalin, and base-catalysed double-bond migration gave 2- [(6-O-α-l-arabinopyranosyl-β- d-glucopyranosyl)oxy ]-3-methylbut-2-enenitrile.     

蔗糖磷酸化酶的研究进展

蔗糖磷酸化酶属于糖苷水解酶13家族,能够催化蔗糖的可逆磷酸解。利用其广泛的底物混杂性,蔗糖磷酸化酶可以将葡萄糖基转移至不同的受体合成熊果苷、甘油葡萄糖苷、低聚糖及多酚化合物的衍生物等产物,这些催化产物可广泛应用于食品、药品、化妆品等行业。随着酶催化技术和蛋白质工程的发展,蔗糖磷酸化酶受到了越来越多的关注,该酶的应用范围也得到了扩大。本文综述了近年来蔗糖磷酸化酶在酶的来源、结构、功能及应用领域等的研究进展,同时讨论了该酶的蛋白质工程改造方法与局限性,并展望了该酶可能的研究方向。     

Glycoside hydrolase family 31 Escherichia coli α-xylosidase

Escherichia coli YicI is a retaining α-xylosidase, which strictly recognizes the α-xylosyl moiety at the non-reducing end, belonging to glycoside hydrolase family 31 (GH 31). We have elucidated key residues determining the substrate specificity at both glycone and aglycone sites of Escherichia coli α-xylosidase (YicI). Detection of distinguishing features between α-xylosidases and α-glucosidases of GH 31 in their close evolutionary relationship has been used for the modification of protein function, converting YicI into an α-glucosidase. Aglycone specificity has been characterized by its transxylosylation ability. YicI exhibits a preference for aldopyranosyl sugars having equatorial 4-OH as the acceptor substrate with 1,6 regioselectivity, resulting in transfer products. The disaccharide transfer products of YicI, α-d-Xylp-(1→6)-d-Manp, α-d-Xylp-(1→6)-d-Fruf, and α-d-Xylp-(1→3)-d-Frup, are novel oligosaccharides, which have never been reported. The transxylosylation products are moderately inhibitory towards intestinal α-glucosidases.     

New ellagitannin and galloyl esters of phenolic glycosides from sapwood of Quercus mongolica var. crispula (Japanese oak)

Two novel glycosides, 4,5-dimethoxy-3-hydroxyphenol 1-O-β-(6′-O-galloyl)-glucopyranoside (1) and (+)-2α-O-galloyl lyoniresinol 3α-O-β-d-xylopyranoside (2), as well as a novel ellagitannin named epiquisqualin B (3), were isolated from sapwood of Quercus mongolica var. crispula along with 19 known phenolic compounds. The structures of the novel compounds were elucidated on the basis of chemical and spectroscopic investigation. Compound 2 is the first example of a lignan galloyl ester, and 3 is the oxidation product of vescalagin, which is the major ellagitannin of this plant.     

cDNA cloning,expression, and enzymatic activity of a novel endogenous cellulase from the beetle Batocera horsfieldi

In this study, we report a novel cellulase [β-1,4-endoglucanase (EGase), EC 3.2.1.4] cDNA (Bh-EGase II) belonging to the glycoside hydrolase family (GHF) 45 from the beetle Batocera horsfieldi. The Bh-EGase II gene spans 720 bp and consists of a single exon coding for 239 amino acid residues. Bh-EGase II showed 93.72% protein sequence identity to Ag-EGase II from the beetle Apriona germari. The GHF 45 catalytic site is conserved in Bh-EGase II. Bh-EGase II has three putative N-glycosylation sites at 56–58 (N–K–S), 99–101 (N–S–T), and 237–239 (N–Y–S), respectively. The cDNA encoding Bh-EGase II was expressed in baculovirus-infected insect BmN cells and Bombyx mori larvae. Recombinant Bh-EGase II from BmN cells and larval hemolymph had an enzymatic activity of approximately 928 U/mg. The enzymatic catalysis of recombinant Bh-EGase II showed the highest activity at 50 °C and pH 6.0.