Special Issue "Thermophilic DNases, RNases and Proteases"
Deadline for manuscript submissions: closed (25 January 2014).
Interests: bacteriophage infectious for refrigerated food spoilage bacteria; fishery microbiology; characterization of microbial proteases and DNases; immunological identification of food borne bacterial pathogens; fermentation technology; production of paralytic shellfish toxins by dinoflagellated algae; production of fish silage and fish hydrolysates; detection of carcinogens in foods; quantitative real-time PCR detection of bacterial pathogenic bacteria in foods
Thermophilic enzymes can be defined as enzymes that are optimally functional at temperatures near or above 45 °C and exhibit little or no enzyme activity at 20 °C. Thermophilic enzymes have a number of unique uses and can also create certain biochemical problems. Nucleases are usually the enemy of the molecular biologist who is involved in preserving the integrity of RNA or DNA samples. However, DNases and RNases do have certain indispensable roles in molecular biology laboratories. Common applications of DNases are: (1) elimination of trace quantities of DNA from glassware, (2) eliminating DNA from RNA preparations, (3) analyzing DNA-protein interactions via DNase footprinting, and (4) nicking DNA prior to radiolabelling by nick translation. In addition, a DNase is now used in the treatment of cystic fibrosis to reduce the viscosity of lung fluids. Ribonucleases are used for (1) eliminating or reducing RNA contamination in plasmid DNA preparations, (2) and mapping mutations in DNA:RNA hybrids by mismatch cleavage at sites of single base mismatches, allowing analysis of cleavage products. The thermal DNase activity present in shellfish tissue can constitute a major problem in PCR detection of bacterial pathogens in shellfish. Recent studies indicate that a thermophilic DNase is capable of notably reducing biofilms produced by Listeria monocytogenes.
Proteases have wide industrial application. Heat tolerant alkaline proteases are commonly added to laundry detergents. The tanning industry uses proteases for dehairing and bating (softening) leather hides. Proteinase K continues to be widely used to digest the peptidogycan of Gram-positive cells to facilitate cell lysis and release of DNA. Proteases are frequently used as meat tenderizers. The ideal meat tenderizing protease should retain some activity during the initial cooking stages so as to reduce the total digestion time.
It is estimated that less than 1% of thermophiic DNases, RNases and proteases produced by microorganisms native to hot springs and oceanic thermal vents have been identified and characterized. In addition, there is a scarcity of data describing thermophilic DNases and RNases from microorganisms in compost heaps. This special issue is designed to elucidate recent studies dealing with thermophilic DNases, RNases and proteases.
Dr. Robert E. Levin
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed Open Access semimonthly journal published by MDPI.
- Thermophilic enzymes
- hot springs
- thermal vents
- compost heaps
- meat tenderizing proteases
- leather bating proteases
- shellfish DNase