The use of an economical medium for the production of alkaline serine proteases by Bacillus licheniformis NH1

The present study is concerned with the selection of new economical media based on agricultural and marine-processing by-products for the production of alkaline proteases by Bacillus licheniformis NH1. Powders from different fish species were prepared and then tested as growth media at a concentration of 10 g/l for proteases production by NH1 strain. Powder prepared from whole Sardinelle was found to be the best substrate for the production of the alkaline protease. The NH1 strain exhibited a slightlygreater protease production (2927 U/ml) in medium containing only whole Sardinelle powder than that obtained in control medium (2800 U/ml). Proteases were produced even when strain NH1 was cultivated in medium containing only powder prepared from combined heads and viscera Sardinelle (CHVSP), about 2117 U/ml. Protease production was also carried out in media containing hulled grain of wheat, a by-product of semolina factories, as carbon source. Maximum activity (2517 U/ml) was achieved when the strain was grown in medium containing hulled grain of wheat (10 g/l), casein peptone (2 g/l), K2HPO4 (0.5 g/l) and KH2PO4 (0.5 g/l). Moreover, protease production was considerably enhanced when thestrain was grown in medium containing both hulled grain of wheat and CHVSP as carbon and nitrogen sources, respectively, (4771 U/ml). The study shows that hulled grain of wheat and powders from fishery by-products could be utilized as bacterial substrates for the production of alkaline proteases by B. licheniformis NH1

Enhancement of Surfactin and Fengycin Production by Bacillus mojavensis A21: Application for Diesel Biodegradation

This work concerns the study of the enhancement of surfactin and fengycin production by B. mojavensis A21 and application of the produced product in diesel biodegradation. The influences of the culture medium and cells immobilization were studied. The highest lipopeptides production was achieved after 72 hours of incubation in a culture medium containing 30 g/L glucose as carbon source and a combination of yeast extract (1 g/L) and glutamic acid (5 g/L) as nitrogen sources with initial pH 7.0 at 30°C and 90% volumetric aeration. The study of primary metabolites production showed mainly the production of acetoin, with a maximum production after 24 h of strain growth. The use of immobilized cells seemed to be a promising method for improving lipopeptides productivity. In fact, the synthesis of both lipopeptides, mainly fengycin, was greatly enhanced by the immobilization of A21 cells. An increase of diesel degradation capacity of approximately 20, 27, and 40% in the presence of 0.5, 1, and 2 g/L of produced lipopeptides, respectively, was observed. Considering these properties, B. mojavensis A21 strain producing a lipopeptide mixture, containing both surfactin and fengycin, may be considered as a potential candidate for future use in bioremediation and crop protection

Purification and structural data of a highly substituted exopolysaccharide from <i>Pseudomonas stutzeri</i> AS22

International audienc

Wound healing and in vitro antioxidant activities of lipopeptidesmixture produced by Bacillus mojavensis A21

peer reviewe

Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Adiguzel, Ahmet/0000-0001-8848-6647WOS: 000396245100008alpha-Amylase from Anoxybacillus thermarum A4 was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration chromatography, with 29.8-fold purification and 74.6% yield. A4 amylase showed best performance for soluble potato starch hydrolysis at 70 degrees C and pH 5.5-10.5. A4 amylase was extremely stable at +4 degrees C, and the enzyme retained over 65% of its original alpha-amylase activity at 70 degrees C and 43% at 90 degrees C. the enzyme's Km values for soluble starch, amylopectin and amylose substrates were obtained as 0.9, 1.3 and 0.5 mg/mL, respectively. EDTA, Hg2+, B4O72-, OH-, CN-, and urea exhibited different inhibition effects; their IC50 values were identified as 8.0, 5.75, 16.5, 15.2, 8.2 and 10.9 mM, respectively. A4 amylase exhibited extreme stability toward some surfactants and perfect match for a wide variety of commercial solid and liquid detergents at 55 degrees C. So, it may be considered to be potential applications for detergent and other industrial uses