Antihypertensive Effect and Safety Evaluation of Rice Bran Hydrolysates from Sang-Yod Rice.

Rice bran hydrolysates contain highly nutritional proteins and beneficial phytochemicals. Sang-Yod rice bran hydrolysates (SRH) extracted from red pigmented rice is a rich source of nutrients and phenolic compounds. The present study evaluated the antihypertensive effect of SRH and its safety in Sprague-Dawley rats. Hypertension was induced in male rats by administration of L-NAME (50 mg/kg/day) in drinking water for three weeks, and the antihypertensive effect of SRH was evaluated. Treatment of SRH (250 or 500 mg/kg) significantly reduced arterial blood pressure and improved hemodynamic parameters. The antihypertensive effect was associated with decreased oxidative stress, suppressed p47phox NADPH oxidase expression, increased nitric oxide bioavailability and decreased angiotensin II level and ACE activity. The SRH was shown to be safe after feeding male and female rats with a rodent diet containing 1.5% SRH for 90 days. Overall, these findings suggest that SRH is safe and may help to prevent hypertension.

Effect of short chain inulin on the rheological and sensory characteristics of reduced fat set coconut milk yoghurt.

The effect of short-chain inulin on the rheological and sensory properties of reduced fat set coconut milk yoghurt was studied with whole fat coconut milk yoghurt as reference. The concentration of short-chain inulin was varied at 0, 5, 10, 15, and 20% w/v respectively. All the yoghurt samples displayed higher elastic modulus G' than viscous modulus G". However, 15% inulin yoghurt had the highest value for G' & G". The 15 and 20% inulin yoghurts displayed high yield stress (1036.7 ± 2.39 & 368.23 ± 0.30 Pa). Addition threshold of 15% was established, beyond this level there was a significant decrease in the yield stress, firmness, cohesiveness and consistency values of the reduced fat yoghurts. Using Pearson correlation analysis, no correlation was observed between firmness and yield stress, Similarly, there was significant correlation between the yield stress and instrumental viscosity r = 0.957; p < 0.01. Furthermore, all yoghurt samples displayed strain thinning behavior except whole fat yoghurt. Carbohydrate was affected by inulin incorporation. Addition of short chain inulin improved sensorial characteristics such as taste, and flavor, but did not display significant difference in color and odor of yoghurt samples. This article is protected by copyright. All rights reserved.

Consistency and solubility changes in herring (Clupea harengus) light muscle homogenates as a function of pH.

Fish muscle proteins can be isolated from a variety of low-value raw materials by solubilization in either acid or base. If the consistency of the resulting solution is sufficiently low, it is possible to recover most of the solubilized proteins and remove most of the lipids by centrifugation. Lipid removal should greatly stabilize the isolated proteins. In a previous investigation into the use of herring for production of these protein isolates, it was observed that this species had particularly high consistency values when the proteins were solubilized. This study was undertaken to determine the consistencies obtained with herring light muscle tissue over the pH range covered by the two processes, from about pH 2.7 to 10.8. Protein solubility was compared to consistency of the resultant solutions. Maximum consistencies of the homogenates, approximately 220 and approximately 175 mPa.s, were obtained at pH values of approximately 3.5 and 10.5, respectively. Consistency began to increase approximately when solubilization began. Storage of homogenates at pH 2.7 decreased the consistency over a 10 min time period. The magnitude of the consistency peaks at both acid and alkaline pH values increased when using ice-stored as well as frozen-stored herring, especially in the acid range. Protein solubility at pH <4 and pH >/=10.8 slightly decreased after post-mortem storage of the herring muscle. It is suggested that the observed changes in consistency result from the expansion and solvation of protein aggregates which eventually dissociate into smaller units, perhaps even monomers.