Objective: Despite the fact that the total energy intake of Japanese people has decreased, the percentage of obese people has increased. This suggests that the timing of meals is related to obesity. The purpose of the study was to investigate the relationship between the timing of meals and obesity, based on analyses of physical measurements, serum biochemical markers, nutrient intake, and lifestyle factors in the context of Chrononutrition.Participants and Methods: We analyzed data derived from 766 residents of Toon City (286 males and 480 females) aged 30 to 79 years who underwent detailed medical examinations between 2011 and 2013. These medical examinations included. (1) physical measurements (waist circumference, blood pressure, etc.); (2) serum biochemical markers (total cholesterol, etc.); (3) a detailed questionnaire concerning lifestyle factors such as family structure and daily habits (22 issues), exercise and eating habits (28 issues), alcohol intake and smoking habits; (4) a food frequency questionnaire based on food groups (FFQg); and (5) a questionnaire concerning the times at which meals and snacks are consumed.Results: The values for body mass index (BMI) and waist circumference were higher for participants who ate dinner less than three hours before bedtime (<3-h group) than those who ate more than three hours before bedtime (>3-h group). The Chi-square test showed that there was a significant difference in eating habits, e.g., eating snacks, eating snacks at night, having dinner after 8 p.m., and having dinner after 9 p.m., between the <3-h group and the >3-h group. Multiple linear regression analysis showed that skipping breakfast significantly influenced both waist circumference (β = 5.271) and BMI (β = 1.440) and that eating dinner <3-h before going to bed only influenced BMI (β = 0.581).Conclusion: Skipping breakfast had a greater influence on both waist circumference and BMI than eating dinner <3-h before going to bed.

Current diagnostic tests such as glycemic indicators have limitations for early detection of impaired glucose tolerance (IGT), which leads to diabetes. Oxidative stress induced by various oxidants in a random and destructive manner is considered to play an important role in the pathophysiology of a number of human disorders and diseases such as impaired glucose tolerance. We have developed an improved method for the measurement of in vivo lipid peroxidation, where the presence of 8-iso-prostaglandin F2α (8-iso-PGF2α), hydroxyoctadecadienoic acids (HODEs), hydroxyeicosatetraenoic acids (HETEs), and 7-hydroxycholesterol (7-OHCh), as well as their parent molecules, linoleic acid (LA) and cholesterol (Ch), was determined by performing LC-MS/MS (for 8-iso-PGF2α, HODE, and HETE) and GC-MS (for 7-OHCh, LA, and Ch) after reduction with triphenyl phosphine and saponification by potassium hydroxide. We then applied this method to volunteers (n = 57), including normal type (n = 43), “high-normal” (fasting plasma glucose, 100–109 mg/dL, n = 7), pre-diabetic type (IGT, n = 5), and diabetic type (n = 2) subjects who are diagnosed by performing oral glucose tolerance tests (OGTTs). Several biomarkers in plasma, such as insulin, leptin, adiponectin, interleukin-6, tumor necrosis factor-α, high sensitivity-C-reactive protein, HbA1c, and glucose levels were measured during OGTT. We found that the fasting levels of (10- and 12-(Z,E)- HODE)/LA increased significantly with increasing levels of HbA1c and glucose during OGTT and with insulin secretion and resistance index. In conclusion, 10- and 12-(Z,E)-HODE may be prominent biomarkers for the early detection of IGT and “high-normal” type without OGTT.

Basidiomycetes were screened for lignin peroxidase (LPO) genes using a DNA probe prepared from the LPO restriction fragment of Phanerochaete chrysosporium. Southern blot analysis showed restriction fragments of chromosomal DNA of Bjerkandera adusta and Coriolus consors hybridized with the probe. Bjerkandera adusta produced LPO in a glucose-peptone medium. Ion-exchange chromatography showed that this fungus produced multiple molecular forms of LPO. One of the enzymes, LPO-2, was purified and characterized. The molecular weight of LPO-2 was 41,000 with a pI of 4.2. Spectral analysis demonstrated that LPO-2 is a haem protein. The enzyme cleaved lignin model dimers mainly at the C alpha-C beta position of the side chain. The LPO-2 exhibited close similarity to LPOs of P. chrysosporium with respect to their basic properties.

Two chromosome-integrating vectors, pLC1 and pLC2, were used. The former is the pUC19-based vector carrying the Lentinus edodes ras gene promoter and priA gene terminator, and the latter is the pBR322-based vector carrying the promoter and terminator of the priA gene. The manganese (II) peroxidase (MnP) cDNA (mnpc) derived from Pleurotus ostreatus was fused between the promoter and terminator of pLC1 and pLC2, yielding the recombinant plasmids pLC1-mnp and pLC2-mnp. These plasmids were introduced into protoplasts of the Coprinus cinereus trp1 strain with the C. cinereus TRP1-containing plasmid pCc1001 by co-transformation. Two Trp+ transformants for each plasmid, showing clearly higher lignin-decolorization activities, were obtained through introduction of pLC1-mnp and pLC2-mnp. Southern-blot analysis revealed that the four transformants all possess the mnpc sequence on their chromosomes. One Trp+ MnP+ transformant (named TF2-7), which was derived from the introduction of pLC2-mnp and carried the highest number of copies (approx. 10) of mnpc, showed remarkably high lignin-decolorization and -degradation activities; at the time of cultivation when only 35%-40% of the lignin was decolored and degraded by the control Trp+ transformant obtained by the introduction of pCc1001 alone, almost all of the lignin was decolored and degraded by TF2-7.

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Laccase from Trametes polyzona WR710-1 was produced under solid-state fermentation using the peel from the Tangerine orange (Citrus reticulata Blanco) as substrate, and purified to homogeneity. This laccase was found to be a monomeric protein with a molecular mass of about 71 kDa estimated by SDS-PAGE. The optimum pH was 2.0 for ABTS, 4.0 for L-DOPA, guaiacol, and catechol, and 5.0 for 2,6-DMP. The K(m) value of the enzyme for the substrate ABTS was 0.15 mM, its corresponding V(max) value was 1.84 mM min(-1), and the k(cat)/K(m) value was about 3960 s(-1)  mM(-1). The enzyme activity was stable between pH 6.0 and 8.0, at temperatures of up to 40 °C. The laccase was inhibited by more than 50% in the presence of 20 mM NaCl, by 95% at 5 mM of Fe(2+), and it was completely inhibited by 0.1 mM NaN(3). The N-terminal amino acid sequence of this laccase is AVTPVADLQISNAGISPDTF, which is highly similar to those of laccases from other white-rot basidiomycetes.

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6-Deoxy-l-glucose, 6-deoxy-l-altrose, and 6-deoxy-l-allose were produced from l-rhamnose with an immobilized enzyme that was partially purified (IE) and an immobilized Escherichia coli recombinant treated with toluene (TT). 6-Deoxy-l-psicose was produced from l-rhamnose by a combination of l-rhamnose isomerase (TT-PsLRhI) and d-tagatose 3-epimerase (TT-PcDTE). The purified 6-deoxy-l-psicose was isomerized to 6-deoxy-l-altrose and 6-deoxy-l-allose with l-arabinose isomerase (TT-EaLAI) and l-ribose isomerase (TT-AcLRI), respectively, and then was epimerized to l-rhamnulose with immobilized d-tagatose 3-epimerase (IE-PcDTE). Following purification, l-rhamnulose was converted to 6-deoxy-l-glucose with d-arabinose isomerase (TT-BpDAI). The equilibrium ratios of 6-deoxy-l-psicose:6-deoxy-l-altrose, 6-deoxy-l-psicose:6-deoxy-l-allose, and l-rhamnulose:6-deoxy-l-glucose were 60:40, 40:60, and 27:73, respectively. The production yields of 6-deoxy-l-glucose, 6-deoxy-l-altrose, and 6-deoxy-l-allose from l-rhamnose were 5.4, 14.6, and 25.1%, respectively. These results indicate that the aldose isomerases used in this study acted on 6-deoxy aldohexoses.