Xu Zirong

Effects of chromium nanoparticle dosage on growth, body composition, serum hormones and tissue chromium in Sprague-Dawley rats *

This 6-week study was conducted to evaluate the effects of seven different levels of dietary chromium (Cr) (0, 75, 150, 300, 450, 600, and 1200 ppb Cr) in the form of Cr nanoparticle (CrNano) on growth, body composition, serum hormones and tissue Cr in Sprague-Dawley (SD) rats. Seventy male SD rats (average initial body weight of (83.2±4.4) g) were randomly assigned to seven dietary treatments (n=10). At the end of the trial, body composition was assessed via dual energy X-ray absorptiometry (DEXA). All rats were then sacrificed to collect samples of blood, organs and tissues for determination of serum hormones and tissue Cr contents. The results indicated that lean body mass was significantly increased (P<0.05) due to the addition of 300 and 450 ppb Cr from CrNano. Supplementation of 150, 300, 450, and 600 ppb Cr decreased (P<0.05) percent body fat significantly. Average daily gain was increased (P<0.05) by addition of 75, 150, and 300 ppb Cr and feed efficiency was increased (P<0.05) by supplementation of 75, 300, and 450 ppb Cr. Addition of 300 and 450 ppb Cr decreased (P<0.05) the insulin level in serum greatly. Cr contents in liver and kidney were greatly increased (P<0.05) by the addition of Cr as CrNano in the dosage of from 150 ppb to 1200 ppb. In addition, Supplementation of 300, 450, and 600 ppb Cr significantly increased (P<0.05) Cr content in the hind leg muscle. These results suggest that supplemental CrNano has beneficial effects on growth performance and body composition, and increases tissue Cr concentration in selected muscles.

Effect of Nano red elemental selenium on GPx activity of broiler chick kidney cellsin vitro

A new selenium source, Nano red elemental selenium (Nano-Se) was used to study the effect on the GPx activity of broiler chick kidney cells (BCKC)in vitro, Sodium selenite (Na2SeO3) and seleno-1-methionine (Se-Met) were used as the controls. The results showed that the effects of three kinds of Se forms on the GPx activity of BCKC were accordant (p>0.05) compared with each other at 0.01. 0.05 and 0.10 μmol/L Se concentrations treatments. In the range of 0.00–0.10 μmol/L Se concentrations, the GPx activity increased with elevation of Se concentrations in medium. For the three kinds of Se forms, the GPx activity reached the climax at 0.10 μmol/L Se concentration. At 0.20 and 0.30 μmol/L Se concentrations, the influnces of three kinds of Se forms were not accordant with one another. For Nano-Se, the GPx activity at 0.20 and 0.30 μmoi/L Se concentrations remained the same as that at 0.10 μmol/L Se concentration treatment. For Se-Met, the GPx activity at 0.20 μmol/L Se concentration treatment remained the same with 0.10 μmol/L treatment; the GPx activity at 0.30 μmol/L Se concentration treatment was declined significantly (p<0.05) compared with 0.10 or 0.20 μmol/L treatment. For Na2SeO3, the GPx activity falled gradually with Se concentration increasing from 0.10 μmol/L to 0.30 μmol/L, and at 0.30 μmol/L Se concentration treatment, the GPx activity was less than the original of BCKC. The results implicated, on the GPx activity of BCKCin vitro, the ranking of width range of the most suitable Se concentration for nutrition curve of the three Se formes is Nano-Se>Se-Met>Na2SeO3.

Purification and some properties of a β-glucanase from a strain,Trichoderma reesei GXC

Abstractβ-glucanase was purified from a solid-state culture ofTrichoderma reesei on wheat bran in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The molecular mass was determined to be 35.21 kilodaltons by sodium dodecyl sulfate-12.5% polyacrylamide gel electrophoresis. The β-glucanase at low pHs was more stable than that at high pHs, and optimum pH was 5.0. The optimum temperature was 60°C, and β-glucanase was relatively stable at below 40°C for 60 min. TheKm of the enzyme on β-glucan was 10.86 mg/ml, and theVmax on β-glucan was 14286 μmol of glucose equivalents per mg of the pure enzyme per min. The β-glucanase activity was significantly inhibited by Fe3+ ions, and was reduced in the presence of Cu2+ ions, Mn2+ ions and Mg2+ ions at 5 mmol/L and 10 mmol/L, respectively. The β-glucanase activity was stimulated by Co2+ ions, Ca2+ ions, Zn2+ ions, and Fe2+ ions at 1 mmol/L and 5 mmol/L, respectively.