Five polysaccharide fractions (AB-1, AB-2, AB-3, AB-4, and AB-5) were obtained after a systemic solvent extraction and precipitation of Agaricus blazei mycelia with yields of 5.20, 9.03, 2.84, 17.47, and 0.44%, respectively. Among which, AB-1 and AB-3 demonstrated great DPPH* radical scavenging ability around 85.0 and 72.0%, respectively, at a concentration of 5 mg/mL. The ferrous ion chelating powers were even more excellent at a concentration of 1 mg/mL, reaching almost over 99.65% for fractions AB-2, AB-3, and AB-4 as compared to the reference control of citric acid (35%); at a dosage of 5 mg/mL, fraction AB-1 even showed 105% in efficiency. In terms of the absolute chelating power (ACP), the mole numbers of ferrous (Fe2+) ions chelated were inversely related with the mean molecular mass of the polysaccharides in each fraction. In addition, gel permeation chromatography analysis showed that the more potent fractions were residing in those fractions with lower molecular masses, such as fractions AB-1 (757 kDa), AB-2 (887 kDa), and AB-4 (631 kDa) etc., and surprisingly, the free radical scavenging capability was also not closely correlated with the mean molecular masses, alternately being well-associated with the solubility of polysaccharides.

Background: Shikimate is essential for protein biosynthesis. Quinate and its derivatives are protective secondary metabolites. Results: Members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. Conclusion:The molecular genetic basis of plant quinate metabolism has been unraveled in vitro. Significance: Identifying quinate metabolic enzymes will allow testing its ecological function and may enable biotechnological applications.

The shikimate pathway synthesizes aromatic amino acids essential for protein biosynthesis. Shikimate dehydrogenase (SDH) is a central enzyme of this primary metabolic pathway, producing shikimate. The structurally similar quinate is a secondary metabolite synthesized by quinate dehydrogenase (QDH). SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, represented here by Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in P. taeda maintained specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displayed a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH was sufficient to gain some QDH function. Thus, very few mutations were necessary to facilitate the evolution of QDH genes.

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Excess summer milk and a lack of product diversity are major problems facing Taiwan's dairy goat industry. Gouda and Mozzarella cheeses made with cow milk are popular products for leisure farms in Taiwan, and they produce a large amount of cheese whey as waste. Our objective is to identify the unstable phenomena of pH-adjusted goat milk through the use of Turbiscan Lab ® Expert and to produce ricotta cheeses using cow cheese whey waste and excess goat milk. Delta backscattering (∆BS) profiles and the Turbiscan stability index (TSI) were used to evaluate the stability characteristics of goat milk adjusted to pH 6.7-5.2. The results show coagulation phenomena in skimmed goat milk and sedimentation phenomena in full-fat goat milk, when the pH was adjusted to 5.2. The TSI values of goat milk at pH 5.7 and 5.2 were significantly higher (p < 0.05) than that of a control. Therefore, 80/20 cow cheese whey/skimmed goat milk and 80/20 cow cheese whey/full-fat goat milk mixtures were acidified to pH 5.5 and heated at 90 • C for 30 min to produce ricotta cheeses A and B. The hardness value, moisture, protein, and ash contents of ricotta cheese A were significantly higher (p < 0.05) than that of ricotta cheese B, but no significant difference was found in terms of sensory evaluation.

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