Lipolytic activity was assayed in samples of Antarctic krill frozen in different conditions and in its liquid digesta with synthetic (tributylglycerol, esters of 2-naphtol and fatty acids C3, C9 , C14 and C18 ) and natural (olive oil) substrates. It was testified that the lipolytic activity is several-fold higher in the crustaceans with high food intake than in those with an empty digestive tract. Krill lipases show higher activity against esters of unsaturated fatty acids that against analogous derivatives of saturated ones and 10-fold higher affinity tributylglycerol (Km = 1.12 mM). Their maximal activity is at pH 6.4 and 37°C. E. superba lipases preserve total activity up to 35°C for 45 minutes, and are completely inactivated at 55°C for 5 minutes. Prevailing part of lipolytic activity is present in krill cephalothorax, however, extracts from krill abdomen also display a marked activity. Krill lipases are probably resistant to an attack of crustacean's proteinases.

Kinetic resolution of (R)- and (S)-mandelic acid by its transesterification with vinyl acetate catalysed by Burholderia cepacia lipase has been studied. The influence of the initial substrate concentration on the kinetics of process has been investigated. A modified ping-pong bi-bi model of enzymatic transesterification of (S)-mandelic acid including substrate inhibition has been developed. The values of kinetic parameters of the model have been estimated. We have shown that the inhibition effect revealed over a certain threshold limit value of the initial concentration of substrate.

As polycarbonate is frequently used in many products, its accumulation in landfi lls is absolutely harmful to the environment. The aims of this study were the screening and isolation of polycarbonate-degrading bacteria (PDB) and the assessment of their ability in the degradation of polycarbonate (PC) polymers. Nine-month buried-PC films were used for PDB isolation and identification. The biodegradation ability of the isolates was determined by growth curve, clear zone formation, lipase and amylase production, AFM and FTIR. Bacillus cereus and Bacillus megaterium were identifi ed and considered as PDB. The degradation ability of B. megaterium was significantly higher than that of B. cereus. Both were lipase and amylase positive. AFM and FTIR results showed the initiation of bacterial attachment. The PC biodegradation ability of isolates can be very efficient. Finding such efficient isolates (which was less studied before) will promise a decrease in plastic contamination in the future.

This study aims at the immobilization and characterization of thermoalkalophilic lipases produced recombinantly from Bacillus thermocatenulatus BTL2 and Bacillus pumilus MBB03. For this purpose, immobilization of the produced enzymes in calcium-alginate@gelatin (Ca–Alg@gelatin) hydrogel beads, immobilization optimization and characterization measurements of the immobilized-enzyme hydrogels were conducted. Optimum temperature and pH values were determined for B. thermocatenulatus and B. pumilus MBB03 immobilized-enzyme hydrogels (60–70 °C, 55 °C and pH 9.5, pH 8.5). Thermal stability was determined between 65 °C and 60 °C of B. thermocatenulatus and B. pumilus MBB03 immobilized enzymes, respectively. The pH stability was determined between pH 7.0–11.0 at +4°C and pH 8.0–10.0 at +4 °C, respectively.
In conclusion, the entrapment technique provided controlled production of small diameter hydrogel beads (~ 0:19 and ~ 0:29) with negligible loss of enzyme. These beads retained high lipase activity at high pH and temperature. The activity of Ca–Alg@gelatin-immobilized lipase remained relatively stable for up to three cycles and then markedly decreased. With this enzyme immobilization, it may have a potential for use in esterification and transesterification reactions carried out in organic solvent environments. We can conclude that it is one of the most promising techniques for highly efficient and economically competent biotechnological processes in the field of biotransformation, diagnostics, pharmaceutical, food and detergent industries.

Background: Despite advanced research and great progress in understanding the chronic pancreatitis (CP) pathogenesis, no current causal treatment for the condition is available. For preclinical studies, the existence of a well-characterized CP animal model is essential.
The aim of the study was to assess the impact of chronic pancreatitis on the antioxidant enzymes activity in rat blood serum and on the level of glutathione (intracellular antioxidant) in rat pancreas.
Methods: The experiments were carried out on the Wistar Kyoto rats in two groups: control and study group (CP), in which chemical induction of pancreatitis with dibutyl dichloride was performed. Serum enzyme activities of amylase, lipase, catalase and superoxide dismutase were analyzed. The levels of the following biochemical parameters were also investigated: total protein, albumin, calcium, magnesium, and triglycerides. Levels of low-molecular-weight thiols: reduced (GSH) and oxidized (GSSG) glutathione, were determined in pancreatic homogenates.
Results: Histopathological imaging of rat pancreatic parenchyma with induced inflammation confirmed focal lymphocytic interstitial chronic pancreatitis with fibrosis features and mild parenchymal atrophy, as well as pancreatic islets degeneration. In the CP group, we observed a statistically significant decrease in serum amylase and lipase activities and in total protein/albumin levels. Also, the elevated catalase activity was registered. In CP rats’ tissues, we observed a 15-fold reduction in GSH levels. The other examined parameters remained unchanged. Clinically relevant are hypoalbuminemia and a moderate decrease in lipase activity. The described changes are most probably indicative of the impaired exocrine pancreas function, however without organ failure features.