Properties of immobilized lipase from Bacillus stearothermophilus MC7. Acidolysis of triolein with caprylic acid

Abstract

Extracellular bacterial lipases are promising biocatalysts for industry, because they are stable and active enzymes from easily available sources. A lipase from Bacillus stearothermophilus MC7 was immobilized on four polymer carriers by physical adsorption: chitosan, DEAE-cellulose, polypropylene, and polyurethane. The four biocatalysts differ in their hydrolytic activity against long-chain and short-chain triglycerides. Lipase MC7 immobilized on polypropylene (PP-MC7) stands out with its high activity against tributirin. According to the preliminary data, all four preparations were suitable for application in the test reaction of acidolysis of triolein with caprylic acid. The highest degree of conversion of the initial triolein was achieved in the presence of PP-MC7 preparation-50%. But variation of the reaction conditions did not lead to synthesis of the target di-substituted product (dicapryloyl-oleoylglycerol, COC). Reaction proceeds as a selective mono-substitution in the glycerol backbone.

Evaluation of a novel thermo-alkaline Staphylococcus aureus lipase for application in detergent formulations

“…Our results revealed that, as opposed to the majority of staphylococcal lipases reported so far (Rosenstein and Gotz, 2000, Sayari et al, 2001, Guncheva et al, 2010), SAL4 lipase is highly stable over a broad pH range and against heat. The highest catalytic activity was indicated at the range of 55–60 °C and pH 12 (Fig.…”

A newly high alkaline lipase: an ideal choice for application in detergent formulations

“…The lipase activity was also determined at different temperatures under optimal conditions (Figure 3C ). In contrast to the majority of staphylococcal lipases described so for [ 3 , 19 , 25 ], the SL1 activity increased significantly with increasing the temperature to reach its maximum value at 60°C. The thermostability of SL1 was also determined by measuring the residual activity after incubation of the pure enzyme at various temperatures (Figure 3D ).…”

“…Lipases (EC 3.1.1.3) represent an important group of biotechnologically valuable enzymes [ 1 - 3 ]. They are widely distributed in nature.…”

Thermostable enzymes and polysaccharides produced by thermophilic bacteria isolated from Bulgarian hot springs

“…The enzyme thermostability was not significantly affected by the immobilization process: when immobilized on DEAE cellulose the enzyme showed a half-life of 37 min at 70°C. Four different polymer carriers were used for acidolysis of triolein with caprylic acid in a selective transesterification reaction [46]. All studied additives slowed down the process of thermal denaturation; an increased enzyme stability was observed for a large number of modifiers applied within a broad concentration range with the highest degree of activation when PEG 6000 was applied (up to 2.3-fold increase) [43].…”

“…The degree of substitution of palmitic acid with oleic acid exceeded 50% after 48 h. The immobilized enzyme exhibited a high operational thermostability with a half-life of 50 days at 60°C in a solvent-free system. Four different polymer carriers were used for acidolysis of triolein with caprylic acid in a selective transesterification reaction [46]. The highest degree of conversion was achieved in the presence of lipase immobilized on polypropylene and only monosubstitution in the glycerol backbone was obtained as a result.…”