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1.
مقالة ي الانجليزية | WPRIM | ID: wpr-1010464

الملخص

An extracellular lipase from Aureobasidium pullulans was obtained and purified with a specific activity of 17.7 U/mg of protein using ultrafiltration and a DEAE-Sepharose Fast Flow column. Characterization of the lipase indicated that it is a novel finding from the species A. pullulans. The molecular weight of the lipase was 39.5 kDa, determined by sodium dodecyl sulfonate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme exhibited its optimum activity at 40 °C and pH of 7. It also showed a remarkable stability in some organic solutions (30%, v/v) including n-propanol, isopropanol, dimethyl sulfoxide (DMSO), and hexane. The catalytic activity of the lipase was enhanced by Ca2+ and was slightly inhibited by Mn2+ and Zn2+ at a concentration of 10 mmol/L. The lipase was activated by the anionic surfactant SDS and the non-ionic surfactants Tween 20, Tween 80, and Triton X-100, but it was drastically inhibited by the cationic surfactant cetyl trimethyl ammonium bromide (CTAB). Furthermore, the lipase was able to hydrolyze a wide variety of edible oils, such as peanut oil, corn oil, sunflower seed oil, sesame oil, and olive oil. Our study indicated that the lipase we obtained is a potential biocatalyst for industrial use.


الموضوعات
Ascomycota/enzymology , Calcium , Catalysis , Corn Oil/metabolism , Detergents/chemistry , Enzyme Stability , Fungal Proteins/chemistry , Glucans/chemistry , Hexanes/chemistry , Hydrogen-Ion Concentration , Hydrolysis , Industrial Microbiology , Lipase/chemistry , Manganese/chemistry , Olive Oil/metabolism , Peanut Oil/metabolism , Sesame Oil/metabolism , Substrate Specificity , Sunflower Oil/metabolism , Surface-Active Agents , Temperature , Zinc/chemistry
2.
مقالة ي الانجليزية | WPRIM | ID: wpr-1010400

الملخص

The storage and transportation of raw milk at low temperatures promote the growth of psychrotrophic bacteria and the production of thermo-stable enzymes, which pose great threats to the quality and shelf-life of dairy products. Though many studies have been carried out on the spoilage potential of psychrotrophic bacteria and the thermo-stabilities of the enzymes they produce, further detailed studies are needed to devise an effective strategy to avoid dairy spoilage. The purpose of this study was to explore the spoilage potential of psychrotrophic bacteria from Chinese raw milk samples at both room temperature (28 °C) and refrigerated temperature (7 °C). Species of Yersinia, Pseudomonas, Serratia, and Chryseobacterium showed high proteolytic activity. The highest proteolytic activity was shown by Yersinia intermedia followed by Pseudomonas fluorescens (d). Lipolytic activity was high in isolates of Acinetobacter, and the highest in Acinetobacter guillouiae. Certain isolates showed positive β-galactosidase and phospholipase activity. Strains belonging to the same species sometimes showed markedly different phenotypic characteristics. Proteases and lipases produced by psychrotrophic bacteria retained activity after heat treatment at 70, 80, or 90 °C, and proteases appeared to be more heat-stable than lipases. For these reasons, thermo-stable spoilage enzymes produced by a high number of psychrotrophic bacterial isolates from raw milk are of major concern to the dairy industry. The results of this study provide valuable data about the spoilage potential of bacterial strains in raw milk and the thermal resistance of the enzymes they produce.


الموضوعات
Animals , Bacteria/genetics , Bacterial Proteins/chemistry , Biofilms , Cold Temperature , Dairy Products , Endopeptidases/chemistry , Enzyme Stability , Food Microbiology , Hot Temperature , Lipase/chemistry , Milk/microbiology , Peptide Hydrolases/chemistry , Phospholipases/chemistry , RNA, Ribosomal, 16S/genetics , Raw Foods/microbiology , beta-Galactosidase/chemistry
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