Evaluation Of Lipase Research Articles

Evaluation of Lipase from an Indigenous Isolated Bacillus Strain for Biodiesel Production

Lipases are utilized in biodiesel production utilizing various types of substrates. The use of lipase in bioenergy production aims to reduce energy crises and environmental pollution. Lipase-producing indigenous bacteria Bacillus licheniformis (Accession no. OP56979) and Bacillus rugosus (Accession no. OP56980) were isolated from various oil-contaminated sites. The isolated potential lipolytic bacteria were screened for maximum lipase production. Then, the bacteria showing the highest lipolytic activity were subjected to identification using the 16s rRNA technique while other isolated were identified biochemically. Lipase [LipBL-WII(c)] from Bacillus licheniformis having the highest lipolytic activity expressed various characteristics. Characterization of crude LipBL-WII(c) expressed that it showed stability in a wide range of pH (4 to 10) with optimum lipolytic activity observed at pH 8. It was then found to be active at a temperature range from 20°C to 80°C with optimal at 50°C. Lipase activity was also stimulated in metal ions such as Ca+1, Mg2+, and Zn2+ the most. Furthermore, LipBL-WII(c) retained lipolytic activity in the presence of various organic solvents and surfactants. The kinetic parameters (Km and Vmax) for LipBL-WII(c) were ascertained using Lineweaver- Burk plot. LipBL-WII(c) showed a potential for biodiesel production using olive oil as a source. Lipase gave 84% yield of biodiesel production from olive oil. Thus, it could be employed as a potential candidate for green biodiesel production using oil sources.

Evaluation of Lipases from Wild Microbial Strains as Biocatalysts in Biodiesel Production

In this study, the evaluation of the catalytic behavior of several wild bacterial strains in the 1,3-selective ethanolysis of triglycerides with ethanol to produce a new type of biodiesel (Ecodiesel) that integrates glycerol as monoacylglycerols was carried out. The Ecodiesel production not only avoids the elimination of glycerol, which is largely generated as a by-product in the biodiesel industry, but also results in an increase in the biofuel yield. The wild microbial strain samples were obtained from several lipophilic organisms. In addition to evaluate the enzymatic extracts, the minimum grade of purification of the strains, necessary to obtain similar results to those attained with commercial lipases was studied. This purification treatment included a dialysis followed by a lyophilization process. Such extracts were directly used as biocatalysts in the transesterification reaction of sunflower oil with ethanol, attaining much better results (yield close to 100%) than those obtained with strains which were not submitted to the purification process (yields lower than 10%). Furthermore, the results here obtained are similar to those obtained with commercial lipases but were achieved under mild conditions and lower reaction time (2 h). In addition, the stability of the enzymatic extracts was corroborated by subsequent reactions, showing no loss of activity. Thus, this study brings to light that enzymatic extracts obtained by a very simple purification process can be economically competitive with the conventional biodiesel production methods.

Evaluation of lipase from Streptomyces variabilis NGP 3 for detergent additive capability

The study was carried out to determine the grease stain removing ability of lipase from an Actinomycete strain (Streptomyces variabilis NGP 3 (JX843530)) recovered from marine sediment of South Indian coastal region. The strain was identified using 16SrRNAgene sequence analysis. The efficiency of lipase produced by Streptomyces variabilis NGP3 in combination with various commercially available detergents (Ariel, Tide, Henko, Rin and Surf excel) was studied. Among them, lipase with Surf excel treated knitted fabric removed 77.27% grease from the fabric. Abrasion resistance test was carried out to analyze the capability of the knitted fabric against abrasion surface. Minimum abrasion of knitted fabric (1.50%) was observed when treated with S. variabilis NGP 3 lipase and surf excel. Perspiration test for the colour fastness of the knitted fabric on treatment with lipase and detergents (Rin and Surf excel) revealed a rating of 5 (ideal) in the Grey scale reader, in both acidic and alkali treatment

Evaluation of lipase from Burkholderia cepacia immobilized in alginate beads and application in the synthesis of banana flavor (isoamyl acetate)

ABSTRACTThe alginate in bead forms was used to immobilize Burkholderia cepacia lipase. The microencapsulation technique for lipase entrapment was a 2% (w/v) of sodium alginate concentration prepared by ionic gelation using calcium chloride as the cross-linking agent in a gelling solution. The beads were tested in different solvents as acetone, chloroform, toluene, n-hexane, and n-heptane. Over a 5-day period (120 h), the n-heptane maintained the reasonable (excellent) residual activity of the immobilized lipase. Morphological studies on reused beads and new beads were performed. All beads for isoamyl acetate yield were tested. The reused bead leaches substantially, with a maximum ester yield of 92%. With modifications in the molar ratios, the synthesis of banana flavor (isoamyl acetate) was performed in both the alcohol per acid and acid per alcohol excesses.

Production of lipase SMG1 and its application in synthesizing diacylglyecrol

Abstract Exploration and evaluation of lipases from different sources will always be required by the swiftly developing industries for modification of oils and fats. Lipase SMG1 from Malassezia globosa was expressed in recombinant Pichia pastoris , and its catalytic activity in the hydrolysis and synthesis of partial glycerides was evaluated. Lipase SMG1 could not hydrolyze soybean oil; however, enhanced the hydrolysis of soybean oil by combining with Palatase 20000L, suggesting it showed strict specificity on mono- and diacylglycerol. Hydrolysates of soybean oil were esterified with glycerol to produce diacylglycerol, and the optimized results for the esterification reaction were with an fatty acids/glycerol molar ratio of 1:4, lipase SMG1 at a concentration of 120 U/g (U/w, with respect to total reactants), initial water content 1% (w/w, with respect to total reactants) and 30 °C, which yielded 62.03% of diacylglycerol in reaction mixture (80.5% in acylglyceride) after 12 h of reaction. The results showed that lipase SMG1 is a prospective enzyme which could be used in the oils and fats industry.

Effects of Starter Diets on Pancreatic Enzyme Activity in Juvenile Sterlet (Acipenser ruthenus)

Nine-day-old sterlet (Acipenser ruthenus) larvae were reared for 21 days on one of three commercial diets with different protein and fat contents: Bio Kyowa, Aglo Norse, or Perla Larva Proactive. At the end of the experiment, the sterlet juveniles were sampled for histological analysis of the pancreas and evaluation of lipase, trypsin, and amylase activity. Fish fed the Bio Kyowa and Aglo Norse diets were the largest. Survival was highest in the Aglo Norse group. There were no differences between groups in histologi- cal analysis of the pancreas, and no histological anomalies. The highest lipase activity was observed in fish fed the diet with the highest lipid content (21%) - the Aglo Norse diet. Trypsin activity was higher in fish fed Bio Kyowa with a protein content of 55% than in fish fed Aglo Norse with a pro- tein content of 59%.

Evaluation of lipases in the desymmetrization of meso-exo-3,5-dihydroxymethylenetricyclo[5.2.1.0(2,6)]decane and the synthesis of chiral derivatives

A dessimetrizacao mais eficiente do composto meso-exo-3,5-dihidroximetilenotriciclo[5.2.1.0 2,6]decano foi com a lipase da Pseudomonas cepacia (PS-C 'Amano' II) em acetato de vinila, quando obteve-se alto rendimento quimico (93%) e excelente excesso enantiomerico (ee > 99%), determinado por cromatografia gasosa em coluna quiral. Desse sistema quiral, foram preparados derivados enantiopuros com potenciais aplicacoes como intermediarios sinteticos.

Toxicological safety evaluation of lipase derived from Rhizopus oryzae

Toxicological safety evaluation of lipase derived from Rhizopus oryzae