1  
[PERSON]  
1 Laboratory of Extremophilic Microorganisms, Department of General Microbiology, The Stephan Angeloff Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Bl. 26, 1113 Sofia, Bulgaria; [EMAIL_ADDRESS] (I.B. ); [EMAIL_ADDRESS] (K.B. ); [EMAIL_ADDRESS] (N.A. ); [EMAIL_ADDRESS] (N.A.) 1  
[PERSON]  
1 Laboratory of Extremophilic Microorganisms, Department of General Microbiology, The Stephan Angeloff Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev StrThere are different sources of pectinases. Bacteria, fungi, yeasts, insects, nematodes, plants, and protozoa have been reported to be producers. Many microbial strain producers are known to possess pectinolytic potential [2]. Bacteria produce mainly alkaline pectinases, while fungi are the major producers of acidic pectinases. The yeasts _Dioszegia_ sp., _Phenolfieria glacialis_, and _Tetracadium_ sp. exhibit pectinase activity at low temperatures [3]. Concerning the industrial sector, acidic pectinases are being used in the extraction and clarification of fruit juices, in winemaking, for the maceration of vegetables and fruits, and for the improvement of essential oil extraction. Various _Aspergillus_ sp. and _Penicillium_ sp. are producers of acidic pectinases [4]. Alkaline pectinases are applied in the pretreatment of pectinaceous waste waters, originating from the food-processing industry. They are also widely utilized in the textile industry for wetting plant fibers, the biopreparation of cotton fabrics, and the enzymatic polishing of cotton-blend fabrics. Alkaline pectinases are mainly produced by _Bacillus_ sp. and _Pseudomonas_ sp. [5]. Today, most of the commercially available and industrially used pectinases are of mesophilic origin, yet extremophilic bacteria have generated much interest due to their extremozymes with unusual properties. Microbial enzyme activity depends on the type of application and conditions, such as temperature, concentration, and pH. Therefore, pectinase enzymes can be differentiated according to physical and chemical factors [6]. Halophilic microorganisms are a source of a variety of extremozymes called halozymes. The conformations of biopolymers are important and can easily be affected. High salt concentrations lead to a reduction in the effective concentration of water and specifically interact with the surfaces of biopolymers [7]. Halozymes work in the presence of organic solvents [8] and extreme values of pH and temperature and salt concentrations--conditions typically encountered in the industrial processes and that generally lead to protein precipitation and denaturation. Biofuel, animal nutrition, detergents, wastewater treatment, food, wine, and beer end-use industries stimulate seeking for industrial extremozymes [9; 10; 11]. Halophiles have biotechnological advantages like a reduced risk of contamination during cultivation, low nutritional requirements, and the ability to utilize a wide range of substances as their sole carbon and energy sources [12]. The solubility of pectin-containing substances at high temperatures and alkaline pH values has sparked interest in searching for novel thermo-alkaliphilic pectinases of extremophilic origin. Although there are many studies related to extremophilic pectinase enzymes produced by thermophilic microorganisms [13; 14], research on pectinases isolated from halophilic producers is still limited [15]. Therefore, it is of interest and importance to find new halophilic sources of pectinases and characterize these enzymes. Representatives of the genus _Virgibacillus_ take part in the different stages of food processing. An example is in the preparation of the traditional salted and fermented Korean food Jeotgal (jeot). An obligatory step is the addition of 20-30% (\(w/v\)) salt to seafood. The main group of microorganisms involved are representatives of the genus _Bacillus_. _Virgibacillus_ and other isolates from the genus _Bacillus_ and related bacteria were isolated, and their potential roles as probiotics were mentioned.