Objective: This study aimed to investigate the effectiveness of a vegetable growing activity in a kindergarten in improving picky eating habits among preschoolers.Methods: This 10-month longitudinal study was conducted in five kindergartens in Hokkaido. Three kindergartens participated in the vegetable growing activity (241 preschoolers; experimental group), while two did not (138 preschoolers; control group). Tomatoes were cultivated. The preschool-ers' mothers provided ratings on a questionnaire before cultivation, after harvesting and six months after harvesting (follow-up). The main outcome investigated was picky eating habits; secondary outcomes were preference for tomato and interest in food and eating. In each group, changes in the answers to these questions were observed, and between-group comparisons were performed on the percentage of preschoolers who had improved picky eating habits.Results: In the experimental group, the percentage of picky eaters decreased significantly after harvesting and follow-up. However, in the control group, the percentage of picky eaters did not change significantly. After harvesting and follow-up, the percentage of preschoolers in the experimental group whose picky eating habits had improved was significantly higher than that of preschoolers in the control group. Furthermore, in the experimental group, the percentage of preschoolers who liked tomatoes, who talked to their mothers happily about vegetables, and who expressed regret for wasting food increased significantly after harvesting or follow-up. However, in the control group, these percentages did not change significantly.
Conclusion:Activities involving growing vegetables such as tomatoes in kindergartens may be beneficial for preschoolers with picky eating habits.Jpn. J. Nutr. Diet., 74 (1) 20~28 (2016)
Twochromones isolated from the methanol extract of glasswort (Salicornia europaea L.) were elucidated to be 7-hydroxy-6-methoxychromoneand 7 O>-/?-D-glucopyranosyl-6-methoxychromone on the basis of chemical and spectral analyses and synthetic studies. These two are natural products hitherto unknown.In a previous paper,1} we have reported that four compounds were isolated from the reddish leaves and stems of glasswort and CompoundsI, II and III were determined to be 2'-hydroxy-6,7-methylenedioxyisoflavone, ( -)-(2S)-2' -hydroxy-6,7-methylenedioxyflavanone and 2/,7-dihydroxy-6-methoxyisoflavone, respectively.
Background:
It has recently been reported that the fruit, stems and leaves of Actinidia arguta have various potential health effects including an antioxidant effect, anticancer effect, anti-allergic effect and α-glucosidase inhibitory effect. However, little is known about the biochemical properties of cysteine protease in the fruit juice of A. arguta.
Methods:
Ion exchange chromatography to purify the cysteine protease from the fruit juice of A. arguta, and some synthetic substrates to determinate the enzyme activity were used.
Results:
Cysteine protease was purified to homogeneity from A. arguta fruit juice by ion exchange chromatography. The molecular weight of the purified enzyme was calculated to be approximately 25,500 by SDS-PAGE in the presence of β-ME. The enzyme rapidly hydrolyzed the substrate Z-Leu-Arg-MCA and moderately hydrolyzed other substrates including Boc-Val-Leu-Lys-MCA, Z-Val-Val-Arg-MCA and Z-Phe-Arg-MCA. Kinetic parameters for these four substrates were determined. The Km, Vmax, Kcat and Kcat/Km values for Z-Leu-Arg-MCA, the most preferentially cleaved by the enzyme, were 100 μM, 63.8 μmoles/mg/min, 27.26 sec-1 and 0.2726 sec-1μM-1, respectively. Furthermore, the activity of the enzyme was strongly inhibited by inhibitors including antipain, leupeptin, E-64, E-64c, kinin-free-LMW kininogen and cystatin C. Those biochemical data indicated that the enzyme was a cysteine protease. The amino acid sequence of the first 21 residues of cysteine protease purified from Actinidia arguta was Val1-Leu-Pro-Asp-Tyr5-Val-Asp-Trp-Arg-Ser10-Ala-Gly-Ala-Val-Val15-Asp-Ile-Lys-Ser-Qln20-Gly. This sequence showed high homology to the sequences of actinidin from Acinidia deliciosa (95.0%) and actinidin from Actinidia eriantha (90%). These three cysteine proteases were thought to be common allied species.
Conclusion:
The biochemical properties of the enzyme purified from A. arguta fruit juice were determined. These basic data are expected to contribute to the maintenance and improvement of human health as well as to the promotion of protein digestion and absorption through its proteolytic functions.
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