Nutritional Potential and Functionality of Whey Powder Influenced by Different Processing Temperature and Storage

Whey is an excellent food ingredient owing to its high nutritive value and its functional properties. However, composition of whey varies depending on composition of milk, processing conditions, processing method, and its whey protein content. The aim of this study was to prepare a whey powder from raw whey and to determine the influence of different processing temperatures (160 and 180 °C) on the physicochemical, functional properties during storage of 180 days and on whey protein denaturation. Results have shown that temperature significantly (P < 0.05) affects the pH, acidity, non-protein nitrogen (NPN), protein total soluble solids, fat and lactose contents. Significantly (p < 0.05) higher foaming capacity (FC), foam stability (FS), whey protein nitrogen index (WPNI), and a lower turbidity and solubility index (SI) were observed in whey powder processed at 160 °C compared to whey powder processed at 180 °C. During storage of 180 days, slow but progressive changes were noticed on the physicochemical and functional properties of whey powder. Reverse phase-HPLC analysis revealed a significant (P < 0.05) effect of temperature on whey protein contents. Denaturation of β-Lactoglobulin is followed by α-lacalbumin, casein glycomacropeptide (CMP/GMP), and bovine serum albumin (BSA).

Isolation and Characterization of Collagen from Chicken Feet

Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient. 

In situ Observation of the State and Stability of Hemoglobin Adsorbed onto Glass Surface by Slab Optical Waveguide (SOWG) Spectroscopy

The state and stability of hemoglobin adsorbed on the glass surface was investigated using slab optical waveguide (SOWG) spectroscopy. The peak position of the absorption band of hemoglobin adsorbed on the glass surface was same as that of the hemoglobin in solution. This result suggests that no significant denaturation occurred by adsorption. The adsorption of hemoglobin is relatively strong that the hemoglobin molecules even remained adsorbed after rinsing the cell with buffer solution. The peak shift caused by the reduction of adsorbed hemoglobin was also observed.

Design and Microfabrication of a High Throughput Thermal Cycling Platform with Various Annealing Temperatures

This study describes a micro device integrated with multi-chamber for polymerase chain reaction (PCR) with different annealing temperatures. The device consists of the reaction polydimethylsiloxane (PDMS) chip, a cover glass chip, and is equipped with cartridge heaters, fans, and thermocouples for temperature control. In this prototype, commercial software is utilized to determine the geometric and operational parameters those are responsible for creating the denaturation, annealing, and extension temperatures within the chip. Two cartridge heaters are placed at two sides of the chip and maintained at two different temperatures to achieve a thermal gradient on the chip during the annealing step. The temperatures on the chip surface are measured via an infrared imager. Some thermocouples inserted into the reaction chambers are used to obtain the transient temperature profiles of the reaction chambers during several thermal cycles. The experimental temperatures compared to the simulated results show a similar trend. This work should be interesting to persons involved in the high-temperature based reactions and genomics or cell analysis.

PTFE Capillary-Based DNA Amplification within an Oscillatory Thermal Cycling Device

This study describes a capillary-based device integrated with the heating and cooling modules for polymerase chain reaction (PCR). The device consists of the reaction polytetrafluoroethylene (PTFE) capillary, the aluminum blocks, and is equipped with two cartridge heaters, a thermoelectric (TE) cooler, a fan, and some thermocouples for temperature control. The cartridge heaters are placed into the heating blocks and maintained at two different temperatures to achieve the denaturation and the extension step. Some thermocouples inserted into the capillary are used to obtain the transient temperature profiles of the reaction sample during thermal cycles. A 483-bp DNA template is amplified successfully in the designed system and the traditional thermal cycler. This work should be interesting to persons involved in the high-temperature based reactions and genomics or cell analysis.

Temperature-dependent Structural Perturbation of Tuna Myoglobin

To unveil the mechanism of fast autooxidation of fish myoglobins, the effect of temperature on the structural change of tuna myoglobin was investigated. Purified myoglobin was subjected to preincubation at 5, 20, 50 and 40oC. Overall helical structural decay through thermal treatment up to 95oC was monitored by circular dichroism spectrometry, while the structural changes around the heme pocket was measured by ultraviolet/visible absorption spectrophotometry. As a result, no essential structural change of myoglobin was observed under 30oC, roughly equivalent to their body temperature, but the structure was clearly damaged at 40oC. The Soret band absorption hardly differed irrespective of preincubation temperature, suggesting that the structure around the heme pocket was not perturbed even after thermal treatment.