Showing 3 results for Lipase
Nasrollahi Omran, A, Nazemi, A, Kihanian, Sh, Aryana , N,
Volume 8, Issue 5 (1-2015)
Abstract
Abstract Background and Objective: With the development of drug resistance in strains of fungi, there is a considerable resistance of Candida albicans strains to fluconazole. Molecular studies are developing to determine the relationship of such a drug resistance with the increased gene expression of enzymes produced in drug-resistant Candida isolates. We aimed to evaluate the relationship between extracellular lipase gene (LIP8) expression of Candida albicans isolated from candidiasis and sensitivity or resistance to fluconazole. Material and Methods: Drug susceptibility of Candida albicans was performed in oral and vaginal candidiasis to determine the proportion of strains sensitive or resistant to fluconazole using NCCLS method. To evaluate and compare the expression of these genes in the susceptible and resistant strains, RT real-time PCR reaction was used. Results: Of 46 Candida albicans, 20 were susceptible, 12 were semi-susceptible and 14 were resistant to fluconazole. By using PCR reaction, the results showed that the expression of this gene in fluconazole-susceptible isolates was moderate, while it was high in the isolates resistant to fluconazole. Conclusion: The results of lipase gene (LIP8) expression showed that the additional expression of some genes of the enzymes responsible for virulence of Candida may also play a role in resistance to fluconazole. Keywords: Candidiasis, Lipase Gene Expression, RT real-time PCR, Fluconazole
Amoozgari, Z, Salehi Pour Bavarsad, S, Noorbehbahani, M,
Volume 9, Issue 1 (4-2015)
Abstract
Abstract
Background and Objective: Snake venom is a complex of several toxic elements and enzymes. It has the agents with the ability to destroy cellular and subcellular membrane and to bring about hemolysis of red blood cells (RBC). Two types of direct and indirect hemolytic activity are known in snake venom in that phospholipase A2 is responsible for the indirect lysis. The aim of this study was to investigate the effect of α-lipoic acid on hemolytic activity of Iranian Vipera Lebetina venom.
Material and Methods: Protein concentration of the crude venom of Vipera Lebetina was determined using bovine serum albumin as a standard. Direct hemolytic activity of venom was determined by using the Human RBC and Indirect hemolytic activity was assayed on RBC in the presence of egg yolk. Then, α-lipoic acid with different concentrations in 100 mM Tris-HCL buffer was applied and its effect on hemolysis of RBC was studied.
Results: direct hemolytic activity on RBC was not observed while its indirect activity was detected to be increased proportional to different concentration of α-lipoic acid. The range of indirect hemolysis was increased up to 60% by 60µm α-lipoic acid.
Conclusion: Not only has α-lipoic acid no inhibitory effects on the hemolytic activity of Iranian Vipera Lebetina venom but also has the positive effects on it.
Keywords: Iranian Vipera Lebetina Venom, Direct Hemolytic, Indirect Hemolytic, α-Lipoic Acid, Phospholipase A2
Neda Gharagozloo Hesari, Davoud Esmaeili, Taher Mohammadian, Mohammad Hasan Shahhosseini, Atousa Ferdosi,
Volume 14, Issue 6 (11-2020)
Abstract
Background and objectives: Industrial wastewater is worldwide health concern. Microorganisms present in the environment have an important role in the biodegradation of lipids, fats and proteins from wastewater. In this regard, microbial lipases and proteases are interesting research targets because of high stability, broad substrate specificity, high yields and availability. In this study, we analyze sequences encoding lipase of Pseudomonas putida and subtilisin of Bacillus subtilis for generation of a new recombinant protein for degradation of environmental contaminations caused by lipids and proteins.
Methods: In this study, sequences of the genes encoding lipase and subtilisin were obtained from GenBank. To predict the 3D structure of the protein, modeling was carried out. The prediction of secondary structure, tertiary structure and solvent accessibility was carried using bioinformatics tools including I-TASSER, GoR4 and ExPasy.
Results: The lipase-subtilisin fusion protein was well-characterized by bioinformatical studies with appropriate spatial and secondary structures. The protein had appropriate hydrophilicity, biological half-life and thermal and acidic stability. The codon optimization was performed appropriately.
Conclusion: Overall, the bioinformatical analysis of the designed protein showed that the recombinant lipase-subtilisin protein has a stable structure both in vitro and in vivo, a negative normalized B-factor and lipolytic and proteolytic activities, which makes it suitable for treatment of lipid and protein contaminations.
