Lipases are hydrolases used in various sectors such as the food, pharmaceutical and chemical synthesis industries. In this study, epiphytic microorganisms were isolated from Serra of Ouro Branco State Park (Minas Gerais, Brazil) subsequently evaluated for their ability to produce extracellular lipases. Among 46 strains, 25 presented positive results lipase production agar plate screening assay....

Cutinases are bacterial and fungal enzymes that catalyze the hydrolysis of natural cutin, a three-dimensional inter-esterified polyester with epoxy-hydroxy fatty acids chain lengths between 16 18 carbon atoms. Due to their ability accept long substrates, cutinases also effective in catalyzing vitro both degradation synthesis several synthetic polyesters polyamides. Here, we present bioinformati...

BACKGROUND There is an increasing interest to seek new enzyme preparations for the development of new products derived from bioprocesses to obtain alternative bio-based materials. In this context, four non-commercial lipases from Pseudomonas species were prepared, immobilized on different low-cost supports, and examined for potential biotechnological applications. RESULTS To reduce costs of e...

Lipases are ubiquitous acyl-hydrolases possessing , canonical folds within their tertiary structures. They all have SerAsp/Glu-His catalytic triad with apparently a cofactor-independent behaviour in their catalysis. The , -hydrolase lipases take part in interfacial catalysis at the lipid-water interface by extending the hydrophobic surface of the catalytic site through a peptide lid or flap...

Lipases have received great attention as industrial biocatalysts in areas like oils and fats processing, detergents, baking, cheese making, surface cleaning, or fine chemistry [1,2]. They can catalyse reactions of insoluble substrates at the lipid-water interface, preserving their catalytic activity in organic solvents [3]. This makes of lipases powerful tools for catalysing not only hydrolysis...

Identification of three overlapping clones in a canine genomic lambda phage library allowed us to determine a detailed restriction enzyme map of the primary transcriptional unit of the pancreatic lipase gene (15.5 kilobase pairs) as well as 15 and 6 kilobase pairs of 5'- and 3'-flanking regions, respectively. DNA sequence analysis provided the primary structure of (a) 1,345 nucleotides (nt) of ...

Triacylglycerol lipases (EC 3.1.1.3) catalyze both hydrolysis and synthesis reactions with a broad spectrum of substrates rendering them especially suitable for many biotechnological applications. Most lipases used today originate from mesophilic organisms and are susceptible to thermal denaturation whereas only few possess high thermotolerance. Here, we report on the identification and charact...

The lipase superfamily includes three vertebrate and three invertebrate (dipteran) proteins that show significant amino acid sequence similarity to one another. The vertebrate proteins are lipoprotein lipase (LPL), hepatic lipase (HL), and pancreatic lipase (PL). The dipteran proteins are Drosophila yolk proteins 1, 2, and 3. We review the relationships among these proteins that have been estab...