ویرایش مقالات انگلیسی- نمونه کار ویرایش

Figures (1 and 2) illustrated the relationship between the denaturation degree and the solubility behavior of WPI at different concentrations (4 -14 w/w) at and pH= (7) after the heat processing of the control and treated samples, respectively. It appearsed that the protein unfolding masked the SH groups for being exposed, and consequently denaturation and phase separation occurred at 5.5% of the protein powder concentration, which could led lead to more severe precipitation with by increasing the protein content.  Hence,  to overcome this problem, the influence effects of different H2O2 concentrations (0.05-4%), protein hydration time (0.5-24 h), the time of treatment by H2O2 (15 min-24 h), homogenizing homogenization speed (5000-25000 rpm), homogenization time (15-120 s), ultrasound amplitude (50-100%) and time (10 – 60 s) were investigated on the stabilization of individual proteins or small aggregated particles was investigated. Interestingly, maximum stability was obtained at an optimized optimal concentration of H2O2 %, when the other individual preparation variables in the mixture accompanied it.

The optimization results (Table 1) suggested that the heat- treated control sample (without H2O2) had a the highest disulfide- induced denaturation and precipitated particles, compared to with the heated control samples in this optimized conditions (Table 1). The results showed that in comparison with their counterparts (gelled ≥ 5.5% w/w), an optimum level of H2O2 was able to improve heat stability during sterilization without any macroscopic aggregation and gelation. In addition, no further aggregation and physical changes were observed during storage (one -month at 4°C). b-Lg is known to be in monomeric form with a net negative charge at pH=7, and the b-Lg gels formed at pH=7 strengthen by intermolecular disulfide bonds.