• Biotechnology and Bioprocess Engineering:BBE
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• v.1 no.1
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• pp.46-50
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• 1996

In order to design industrial scale reactors and proceises for multi-phase biocatalytic reactions, it is essential to understand the mechanisms by which such systems operate. To il-lustrate how such mechanisms can be modeled, the hydrolysis of the primary ester groups of triglycerides to produce fatty acids and monoglycerides by lipased (glycerol-ester hydrolase) catalysis has been selected as an example of multiphase biocatalysis. Lipase is specific in its behavior such that it can act only on the hydrolyzed (or emulsified) part of the substrate. This follows because the active center of the enzyme is catalytically active only when the substrate contacts it in its hydrolyzed form. In other words, lipase acts only when it can shuttleback and forth between the emulsion phase and the water phase, presumably within an interphase or boundary layer between these two phases. In industrial applications lipase is employed as a fat splitting enzyme to remove fat stains from fabrics, in making cheese, to flavor milk products, and to degrade fats in waste products. Effective use of lipase in these processes requires a fundamental understanding of its kinetic behavior and interactions with substrates under various environmental conditions. Therefore, this study focuses on modeling and simulating the enzymatic activity of the lipase as a step towards the basic understanding of multi-phase biocatalysis processes.

• Journal of Microbiology and Biotechnology
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• v.24 no.10
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• pp.1382-1388
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• 2014

Proteus vulgaris K80 lipase was expressed in Escherichia coli BL21 (DE3) cells and immobilized on amine-terminated magnetic microparticles (Mag-MPs). The immobilization yield and activity retention were 84.15% and 7.87%, respectively. A homology model of lipase K80 was constructed using P. mirabilis lipase as the template. Many lysine residues were located on the protein surface, remote from active sites. The biochemical characteristics of immobilized lipase K80 were compared with the soluble free form of lipase K80. The optimum temperature of K80-Mag-MPs was $60^{\circ}C$, which was $20^{\circ}C$ higher than that of the soluble form. K80-Mag-MPs also tended to be more stable than the soluble form at elevated temperatures and a broad range of pH. K80-Mag-MP maintained its stable form at up to $40^{\circ}C$ and in a pH range of 5.0-10.0, whereas soluble K80 maintained its activity up to $35^{\circ}C$ and pH 6.0-10.0. K80-Mag-MPs had broader substrate specificity compared with that of soluble K80. K80-Mag-MPs showed about 80% residual relative activity after five recovery trials. These results indicate the potential benefit of K80-Mag-MPs as a biocatalyst in various industries.

• Archives of Pharmacal Research
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• v.27 no.10
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• pp.1048-1052
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• 2004

A 1, 2-diglyceride-based multi-step colorimetric assay to measure the pancreatic lipase activity was applied for the determination of the kinetic profiles of the lipase inhibition with a slight modification and the validity verification. With this assay method, our study revealed that platycodin D, one of major constituents of Platycodi Radix, inhibits the pancreatic lipase activity in a competitive type, with the value of $K_I$ being 0.18${\pm}$0.02 mM. In addition, PD has affected the values of $K_{m,app}\;and\;K_{cat}/K_m$ in a dose- dependent manner. The results shed a meaningful light on how PD mediates lipid metabolism in the intestinal tracts. On the other hand, since the revised assay is sensitive, rapid, and does not affect the accuracy to the kinetic properties, it is applicable not only to evaluation of the kinetic properties of the pancreatic lipase, but also to highthroughput screening of pancreatic lipase activity.

• Journal of Physiology & Pathology in Korean Medicine
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• v.19 no.3
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• pp.710-715
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• 2005

This research was to investigate inhibitory activity of Sasang medicines on Obesity. 56 kind of herb medicines to powder, abstract add 100 times methanol. Examine inhibitory effect against lipase activity in vitro. It was compared Xenical(Orlistat) with 56 kind of herb medicines. Inhibitory effect against lipase activity of Xenical as a standard was 93.3%. It is Inhibitory effect against lipase activity of Taeyangin herb medicine. (Fructus Pruni Tomentosae 77.7% Cortex Acanthopanacis73.5%, Fructus Chaenomelis73.1%, rice bran on a mallet head68.1%, Semen Fagopyri 48.1%, Radix Vitis 31.5%) It is Inhibitory effect against lipase activity of Soyangin herb medicine. (Radix Saposhnikoviae 91.5%, Semen Plantaginis 90.4%, Semen Trichosanthis 89.2%, Herba Schizonepetae 85.7%, Radix Euphorbiae Kansui 76.1%, Rhizoma Anemarrhenae 76.0%, Cortex Phellodendri 75.1%, Herba Menthae 74.8%, Radix Angelicae Pubescentis 61.2%, Rhizoma Alismatis 62.6%, Poria 60.9%, Rhizoma Notopterygii 22.5%, Radix Peucedani 18.2%, Caulis Akebiae 17.7%) It is Inhibitory effect against lipase activity of Taeeumin herb medicine. (Herba Spirodelae 91.4%, Radix Polygalae 88.3%, Arillus Longanae 84.3%, Radix Platycodi 81.7%, Semen Zizyphi Spinosae 80.2%, Spina Gleditsiae 79.7%, Herba Ephedrae 75.3%, Semen Raphani 73.1%, Rhizoma Cimicifugae 73.0%, Rhizoma Acori Graminei 71.8%, Flos Chrysanthemi71.0%, Radix et Rhizoma Rhei 68.4%, Vermiculus Holotrichia 59.9%, Radix Puerariae 55.3%, Fructus Schizandrae 53.4% Semen Coicis 50.6%, Semen Biotae 47.5%, Semen Nelumbinis 46.7%, Radix Angelicae Dahuricae 45.1%, Semen Castaneae 44.4%, Rhizoma Ligustici 34.5%, Tuber Liriopis 16.4%, Radix Scutellariae4.2%) It is Inhibitory effect against lipase activity of Soeumin herb medicine. (Pericarpium Arecae89.9%, Rhizoma Alpiniae Officinarum 89.5%, Radix Polygoni Multiflori81.2%, Rhizoma Cyperi 79.0%, Cortex Magnoliae 72.8%, Radix Aucklandiae 72.0%, Rhizoma Zingiberis 71.9%, Pericarpium Citri Reticulatae Viride 71.3%, Radix Cynanchi Wilfordi 57.7% Rhizoma Pinelliae 36.7%, Fructus Alpiniae Oxyphyllae 35.8% Fructus Aurantii Immaturus 17.5%, Pericarpium Citri 16.1%) Therefore, Radix Saposhnikoviae(91.5) and Herba Spirodelae(91.4%) were the most effective medicice of 56 kind of medicines.

• BMB Reports
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• v.41 no.3
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• pp.254-258
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• 2008

Lipase was purified from squid (Todarodes pacificus) liver in an attempt to investigate the possibility of applying the enzyme for biotechnological applications. Crude extract of squid liver was initially fractionated by the batch type ion exchange chromatography. The fraction containing lipase activity was further purified with an octyl-Sepharose column. Finally, lipase was purified by eluting active protein from a non-dissociating polyacrylamide gel after zymographic analysis. Molecular weight of the purified enzyme was determined to be 27 kDa by SDS-polyacrylamide gel electrophoresis. The enzyme showed the highest activity at a temperature range of $35-40^{\circ}C$ and at pH 8.0. The activity was almost completely inhibited at 1 mM concentration of $Hg^{2+}$ or $Cu^{2+}$ ion. Partial amino acid sequence of the enzyme was also determined.

• BMB Reports
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• v.36 no.4
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• pp.417-420
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• 2003

The present work describes a colorimetric microplate assay for lipase activity based on the reaction between 5,5'-dithiobis(2-nitro benzoic acid) (DTNB) and the hydrolysis product of 2,3-dimercapto-1-propanol tributyrate (DMPTB). Reaction mixtures containing DTNB, DMPTB, and lipase were prepared in microplate wells, and the absorbance at 405nm was recorded after incubation at $37^{\circ}C$ for 30 min. A linear relationship was obtained in the range of 0.1-1 U of lipase activity by this method. The reaction conditions were also optimized for the range of 0.01-0.1 U or 1-10 U. When assaying crude tissue extracts, the reaction of DTNB with non-specific reducing agents created a major source of error. However, this error was corrected by the use of blank samples that did not contain DMPTB.

• The Korean Journal of Food And Nutrition
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• v.22 no.1
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• pp.14-19
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• 2009

This study was performed to characterize the lipases produced from Gelidibacter sp. YH333 and Vibrio sp. YH339 isolated from mud flats for industrial application of a lipase. Amount of the lipases secreted from the isolated strains was sharply increased in the proportion of increase of number of the cells. The lipases produced from the isolated strains were constitutively secreted from the cells. The lipase activity of Gelidibacter sp. YH333 was higher than that of Vibrio sp. YH339 to p-nitrophenyl esters. The lipases produced from both strains showed the highest activity in p-nitrophenyl laulate among various p-nitrophenyl esters. The molecular weights of the lipases from Gelidibacter sp. YH333 were about 50 KDa and 25 KDa, respectively. Molecular weight of the lipase from Vibrio sp. YH339 was about 50 KDa.

• Mycobiology
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• v.51 no.1
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• pp.60-66
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• 2023

In this study, the α-amylase inhibitory activity, α-glucosidase inhibitory activity, pancreatic lipase inhibitory activity, and Xanthine Oxidase inhibitory activity of the fruiting body extracts of 5 varieties of Agaricus bisporus (AB) were confirmed. First, the α-amylase inhibitory activity of AB12, AB13, AB18, AB34, and AB40 methanol extracts was lower than that of acarbose, a positive control, in all concentration ranges. The α-glucosidase inhibitory activity of the AB40, AB13, and AB12 methanol extracts at the extract concentration of 1.0 mg/mL was 80.5%, 81.3%, and 78.5%, respectively, similar to that of acarbose, a positive control. The pancreatic lipase inhibitory activity of the methanol extract of Agaricus bisporus fruiting body was significantly lower than that of the positive control orlistat in the concentration range of 50~1.000 (mg/mL). The Xanthine Oxidase inhibitory activity was 0.5~8.0 mg/mL of each extract, which was significantly lower than that of the positive control allopurinol in the same concentration range. However, the Xanthine Oxidase inhibitory activity of AB13 and AB40 at 8.0 mg/mL was about 70%, which was higher than that of other mushrooms. In conclusion, five kinds of Agaricus bisporus fruiting bodies seem to have inhibitory effects on enzymes such as α-amylase, α-glucosidase, pancreatic lipase, and Xanthine Oxidase that degrade starch and protein. In particular, it has an inhibitory effect and a reduction effect on xanthine oxidase that causes gout, so it is expected that it can be developed and used as a food or health supplement with health functional properties through future research.

• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.191-196
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• 1998

This mini review describes the effects of water activity (${\alpha}_w$) on the kinetics, regio- and enantioselectivities of lipases, and various methods for measuring and controlling ${\alpha}_w$ in lipase catalyzed reaction in organic solvent.

• Microbiology and Biotechnology Letters
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• v.50 no.1
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• pp.71-80
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• 2022

Lipases (triacylglycerol acylhydrolases [EC 3.1.1.3]) are water-soluble enzymes. They catalyze the hydrolysis of fats and oils. A cold-active lipase from marine Bacillus cereus HSS, isolated from the Mediterranean Sea, Alexandria, Egypt, was purified and characterized. The total purification depending on lipase activity was 438.9 fold purification recording 632 U/mg protein. The molecular weight of the purified lipase was estimated to be 65 kDa using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The optimum substrate concentration, enzyme concentration, pH, and temperature were 1.5 mM, 100 µl, pH 6 and 10℃, respectively. The lipase was tolerant to NaCl concentrations ranging from 1.5 to 4.5%. The lipase was affected by the tested metal ions, and its activity was inhibited by 16% in the presence of 0.05 M SDS. The application of the cold-active lipase for the removal of an oil stain from a white cotton cloth showed that it is a promising biological agent for the treatment of oily wastes and other related applications. To the best of our knowledge, this is the first report of the purification and characterization of a lipase from marine B. cereus HSS isolated from the Mediterranean Sea.