Physicochemical Properties and Whey Proteomes of Camel Milk Powders Produced by Different Concentration and Dehydration Processes.

Camel milk powder production is an alternative to preserve the perishable milk for later-date consumption. However, the impacts of dehydration processes on bioactive compounds in camel milk are largely unknown. Hence, the present study attempted to compare the physicochemical properties and protein profiles of camel milk powders produced by different concentration and dehydration processes.

Camel milk: A review of its nutritional value, heat stability, and potential food products.

Camel milk is superior to bovine milk and quite close to human milk in terms of its nutritional value. It contains high concentrations of many bioactive compounds that are essential for human health. Despite its profound nutritional and health benefits, food products produced from camel milk are still very limited compared to bovine milk.

Comprehensive biochemical and proteomic characterization of seasonal Australian camel milk.

Although camel milk is increasingly becoming a popular alternative to bovine milk around the world including Australia, studies of Australian camel milk are still lacking. A comprehensive and systematic analysis of major nutritional components, physical properties, antimicrobial enzymes and whey proteomes of Australian camel milk obtained over four seasons was conducted, for the first time in present study. The composition and physical properties of Australian camel milk varied with season, milking frequency and yield.

Digestibility of proteins in camel milk in comparison to bovine and human milk using an in vitro infant gastrointestinal digestion system.

The absence of β-lactoglobulin, high β-/α-casein ratio and protective proteins make camel milk a promising alternative protein base for making human infant formulae. In this study, protein digestibility of camel milk was compared with that of bovine and human milk using an in vitro infant gastrointestinal digestion system. A low degree of gastric proteolysis was observed in all three kinds of milk, and a single clot was formed in camel milk.

A sensitive, high-throughput fluorescent method for the determination of lactoperoxidase activities in milk and comparison in human, bovine, goat and camel milk.

Lactoperoxidase (LPO) is one of the major antibacterial ingredients in milk and an extensively employed indicator for milk heat treatment. The traditional method for LPO activity measurement using ABTS (2,2'-azinobis(3-ethylbenzothiazoline-6-sulphonate) cannot achieve high sensitivity and is affected by indigenous milk thiocyanate. A more sensitive microplate fluorescent assay was developed by monitoring generation of red-fluorescent resorufin from LPO catalysed oxidation of Amplex® Red (1-(3,7-dihydroxyphenoxazin-10-yl)ethanone) in this study.

A sensitive and high-throughput fluorescent method for determination of oxidase activities in human, bovine, goat and camel milk.

Milk oxidases are an integral part of milk immune system, and good indicators for milk thermal history. Current assay methods for milk oxidases are either insensitive, tedious or not cost-effective. In this study, a high-throughput fluorescence assay method for determination of xanthine oxidase (XO) and polyamine oxidase (PAO) activities in milk samples was developed.

A Genome-Wide Prediction and Identification of Intergenic Small RNAs by Comparative Analysis in 7653R.

In bacteria, small non-coding RNAs (sRNAs) are critical regulators of cellular adaptation to changes in metabolism, physiology, or the external environment. In the last decade, more than 2000 of sRNA families have been reported in the Rfam database and have been shown to exert various regulatory functions in bacterial transcription and translation. However, little is known about sRNAs and their functions in .

Identification and Characterization of a New Alkaline Thermolysin-Like Protease, BtsTLP1, from Bacillus thuringiensis Serovar Sichuansis Strain MC28.

Thermolysin and its homologs are a group of metalloproteases that have been widely used in both therapeutic and biotechnological applications. We here report the identification and characterization of a novel thermolysin-like protease, BtsTLP1, from insect pathogen Bacillus thuringiensis serovar Sichuansis strain MC28. BtsTLP1 is extracellularly produced in Bacillus subtilis, and the active protein was purified via successive chromatographic steps.

A new thermostable β-glucosidase mined from Dictyoglomus thermophilum: properties and performance in octyl glucoside synthesis at high temperatures.

A new β-glucosidase (DtGH) representing 40% identity with an apple seed glycosidase (ASG) was cloned from Dictyoglomus thermophilum. DtGH showed extremely high thermostability in aqueous solution, with half-lives of 533, 44, and 5 h measured at 70, 80 and 90 °C, respectively. Therefore it was used for direct glycosylation of n-octanol at 70 °C instead of 50 °C as usually.