Processing Challenges and Opportunities of Camel Dairy Products

A review on the challenges and opportunities of processing camel milk into dairy products is provided with an objective of exploring the challenges of processing and assessing the opportunities for developing functional products from camel milk. The gross composition of camel milk is similar to bovine milk. Nonetheless, the relative composition, distribution, and the molecular structure of the milk components are reported to be different. Consequently, manufacturing of camel dairy products such as cheese, yoghurt, or butter using the same technology as for dairy products from bovine milk can result in processing difficulties and products of inferior quality. However, scientific evidence points to the possibility of transforming camel milk into products by optimization of the processing parameters. Additionally, camel milk has traditionally been used for its medicinal values and recent scientific studies confirm that it is a rich source of bioactive, antimicrobial, and antioxidant substances. The current literature concerning product design and functional potential of camel milk is fragmented in terms of time, place, and depth of the research. Therefore, it is essential to understand the fundamental features of camel milk and initiate detailed multidisciplinary research to fully explore and utilize its functional and technological properties

Dissection of the antimicrobial and hemolytic activity of Cap18: Generation of Cap18 derivatives with enhanced specificity

<div><p>Due to the rapid emergence of resistance to classical antibiotics, novel antimicrobial compounds are needed. It is desirable to selectively kill pathogenic bacteria without targeting other beneficial bacteria in order to prevent the negative clinical consequences caused by many broad-spectrum antibiotics as well as reducing the development of antibiotic resistance. Antimicrobial peptides (AMPs) represent an alternative to classical antibiotics and it has been previously demonstrated that Cap18 has high antimicrobial activity against a broad range of bacterial species. In this study we report the design of a positional scanning library consisting of 696 Cap18 derivatives and the subsequent screening for antimicrobial activity against <i>Y</i>. <i>ruckeri</i>, <i>A</i>. <i>salmonicida</i>, <i>S</i>. Typhimurium and <i>L</i>. <i>lactis</i> as well as for hemolytic activity measuring the hemoglobin release of horse erythrocytes. We show that the hydrophobic face of Cap18, in particular I13, L17 and I24, is essential for its antimicrobial activity against <i>S</i>. Typhimurium, <i>Y</i>. <i>ruckeri</i>, <i>A</i>. <i>salmonicida</i>, <i>E</i>. <i>coli</i>, <i>P</i>. <i>aeruginosa</i>, <i>L</i>. <i>lactis</i>, <i>L</i>. <i>monocytogenes</i> and <i>E</i>. <i>faecalis</i>. In particular, Cap18 derivatives harboring a I13D, L17D, L17P, I24D or I24N substitution lost their antimicrobial activity against any of the tested bacterial strains. In addition, we were able to generate species-specific Cap18 derivatives by particular amino acid substitutions either in the hydrophobic face at positions L6, L17, I20, and I27, or in the hydrophilic face at positions K16 and K18. Finally, our data showed the proline residue at position 29 to be essential for the inherent low hemolytic activity of Cap18 and that substitution of the residues K16, K23, or G21 by any hydrophobic residues enhances the hemolytic activity. This study demonstrates the potential of generating species-specific AMPs for the selective elimination of bacterial pathogens.</p></div