Abstract: 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).
Abstract: 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.
Abstract: 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.
Abstract: 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.
Abstract: 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.
Abstract: 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.