Calorimetric and spectroscopic investigations of β-lactoglobulin upon interaction with copper ion

The effect of copper(II) ions (Cu(+2)) on the structure of β-lactoglobulin (β-lg) was investigated spectroscopically using UV-visible, fluorescence and circular dichroism (CD) and calorimetrically using isothermal titration calorimetry (ITC), at different temperatures. Results of the UV-visible studies showed that adding Cu(+2) to β-lg solution caused increasing turbidity, indicative of protein aggregation. It was noticeable that the rate of increasing turbidity was directly proportional to increasing temperature. The far-UV CD studies displayed that the Cu(+2) cannot induce any significant changes in the secondary structures of β-lg at different temperatures. Also, the ITC data indicated that the binding process of Cu(+2) to β-lg is mainly entropically driven. The results highlight that copper ions cause the tertiary structure of β-lg to change and induce a slightly open structure leading to the formation of supramolecular aggregates in β-lg which may result in the reduced allergenicity of β-lg and its increased use in industrial applications.     

Analytical overview of DNA interaction with Morin and its metal complexes

Flavonoids play an important role in pharmaceutical and biomedical sciences. Various flavonoids, especially Morin, have potential to interact with DNA. Their prospective clinical and pharmacological utilities have attracted researchers?? attention in last two decades. Due to their interaction with DNA and their anticancer effects, a lot of investigations have been carried out all over the world. In this paper, we will review the properties of Morin and its different metal complexes as well as their interactions with DNA that have been reported by several research groups. Also, further details have been provided about binding mechanisms of these materials with DNA using analytical techniques such as UV?CVisible and fluorescence spectroscopies, viscosity and voltammetry. Structural analysis showed Morin binds to DNA through non-intercalation mode, but its metal complexes interact with DNA via intercalation mode and binding mode of Morin, and its metal complexes with DNA will be helpful in the determination of anticancer drugs binding mechanism to DNA. Therefore, it will be useful in new drug designs.     

Short communication: Molecular characteristics,antimicrobial susceptibility,and pathogenicity of clinical Nocardia cyriacigeorgica isolates from an outbreak of bovine mastitis

The occurrence of nocardial mastitis, mostly in the context of outbreaks, has been reported in many countries. However, there is a paucity of reports regarding detailed characterization of Nocardia cyriacigeorgica from bovine mastitis. Thus, herein we report characteristics, antimicrobial susceptibility patterns, molecular identification, and pathogenicity of N. cyriacigeorgica isolated from an outbreak of clinical mastitis in a dairy herd in northern China. A total of 182 (80.2%) lactating cows had clinical mastitis with severe inflammation and firmness of the udder, reduced milk production, and anorexia, with no apparent clinical response to common antibiotics. Out of 22 mastitic milk samples submitted to our laboratory, 12 N. cyriacigeorgica were isolated and characterized using standard microbiological analysis, 16S rRNA gene sequencing, random amplified polymorphic DNA PCR analysis, biochemical assays, and antibiotic susceptibility testing. Additionally, in vivo experiments were done to determine pathogenicity of these clinical mastitis isolates. All isolates were resistant to ampicillin, amoxicillin-clavulanic acid, ciprofloxacin, minocycline, rifampicin, and aminoglycosides (type VI pattern). Additionally, intramammary inoculation of mice with N. cyriacigeorgica caused chronic inflammatory changes, including hyperemia, edema, and infiltration of lymphocytes and neutrophils, as well as hyperplasia of lymph nodules in mammary glands. Therefore, we concluded that N. cyriacigeorgica was involved in the current outbreak of mastitis. To our best knowledge, this is the first report to characterize N. cyriacigeorgica isolated from cases of bovine mastitis in China.     

Cheddar Cheese Ripening and Flavor Characterization: A Review

Cheddar cheese is a biochemically dynamic product that undergoes significant changes during ripening. Freshly made curds of various cheese varieties have bland and largely similar flavors and aroma and, during ripening, flavoring compounds are produced that are characteristic of each variety. The biochemical changes occurring during ripening are grouped into primary events including glycolysis, lipolysis, and proteolysis followed by secondary biochemical changes such as metabolism of fatty acids and amino acids which are important for the production of secondary metabolites, including a number of compounds necessary for flavor development. A key feature of cheese manufacture is the metabolism of lactose to lactate by selected cultures of lactic acid bacteria. The rate and extent of acidification influence the initial texture of the curd by controlling the rate of demineralization. The degree of lipolysis in cheese depends on the variety of cheese and may vary from slight to extensive; however, proteolysis is the most complex of the primary events during cheese ripening, especially in Cheddar-type cheese.     

The physicochemical parameters during dry heating strongly influence the gelling properties of whey proteins

In this study we determined the composition (proportion of native proteins, soluble and insoluble aggregates) and quantified the gelling properties (gel strength and water holding capacity) of pre-texturized whey proteins by dry heating under controlled physicochemical conditions. For this purpose, a commercial whey protein isolate was dry heated at 80 °C (up to 6 days), 100 °C (up to 24 h) and 120 °C (up to 3 h) under controlled pH (2.5, 4.5 or 6.5) and water activity (0.23, 0.32, or 0.52). Gelling properties were quantified on heat-set gels prepared from reconstituted pre-texturized proteins at 10% and pH 7.0. The formation of dry-heat soluble aggregates enhanced the gelling properties of whey proteins. The maximal gelling properties was achieved earlier by increasing pH and water activity of powders subjected to dry heating. An optimized combination of the dry heating parameters will help to achieve better gelling properties for dry heated whey proteins.