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3.1.1.3

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Showing 1-30 of 46 results for "3.1.1.3 " within Papers
R Sharma et al.
Biotechnology advances, 19(8), 627-662 (2003-10-11)
Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. Lipases occur widely in nature, but only microbial lipases are commercially significant. The many applications of lipases include speciality organic
R C Davis et al.
Genomics, 10(1), 262-265 (1991-05-01)
Pancreatic colipase is a 12-kDa polypeptide cofactor for pancreatic lipase (EC 3.1.1.3), an enzyme essential for the absorption of dietary long-chain triglyceride fatty acids. Colipase is thought to anchor lipase noncovalently to the surface of lipid micelles, counteracting the destabilizing
Petra Slanc et al.
Phytotherapy research : PTR, 23(6), 874-877 (2008-12-25)
Lipids are important components in human nutrition; however, their increased intake contributes to the development of obesity and can lead to multiple long-term complications. Pancreatic lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) is a key enzyme for the absorption of dietary triglycerides.
Renata Kołodziejska et al.
Chirality, 30(2), 206-214 (2017-11-16)
The application of ionic liquids as solvents for transesterification of prochiral pirymidine acyclonucleoside using lipase (EC 3.1.1.3) Amano PS from Burkholderia cepacia (BCL) is reported. The effect of using medium reaction, acyl group donor, and temperature on the activity and
P Lohse et al.
Journal of lipid research, 38(5), 880-891 (1997-05-01)
Human gastric lipase (HGL; triacylglycerol lipase; EC 3.1.1.3) plays an important role in the digestion of dietary triglycerides in the gastrointestinal tract, especially in patients suffering from pancreatic lipase deficiencies. The enzyme is secreted by the fundic mucosa of the
W Stuer et al.
Journal of bacteriology, 168(3), 1070-1074 (1986-12-01)
Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was excreted by Pseudomonas aeruginosa PAC1R during the late logarithmic growth phase. Characterization of cell-free culture supernatants by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of significant amounts of lipopolysaccharide, part of which seemed
Hong Li et al.
Endocrinology, 143(9), 3333-3340 (2002-08-24)
Hormone-sensitive lipase (HSL, E.C.3.1.1.3, gene designation Lipe) is reportedly the major cholesteryl esterase of adrenal cortex. Because of the potential importance of cholesteryl ester hydrolysis in steroidogenesis, gene-targeted HSL-deficient mice were assessed for adrenal cortical morphology and function. Compared with
Ki Hyun Nam et al.
Biochemical and biophysical research communications, 389(2), 247-250 (2009-09-01)
The esterase/lipase family (EC 3.1.1.3/EC 3.1.1.1) represents a diverse group of hydrolases that catalyze the cleavage of ester bonds and are widely distributed in animals, plants and microorganisms. Among these enzymes, hormone-sensitive lipases, play a critical role in the regulation
S G Bhavya et al.
Biotechnology progress, 28(6), 1542-1550 (2012-09-27)
This work deals with the downstream processing of lipase (EC 3.1.1.3, from Aspergillus niger) using liquid emulsion membrane (LEM) containing reverse micelles for the first time. The membrane phase consisted of surfactants [cetyltrimethylammonium bromide (CTAB) and Span 80] and cosolvents
Ivana Leščić Ašler et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 11), 1378-1381 (2011-11-22)
A recombinant lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) from the bacterium Streptomyces rimosus was inhibited by the serine protease inhibitor 3,4-dichloroisocoumarin and crystallized by the hanging-drop vapour-diffusion method at 291 K. The crystals belonged to the monoclinic space group P2(1), with
C M Romero et al.
Colloids and surfaces. B, Biointerfaces, 172, 699-707 (2018-09-25)
Lipases (EC 3.1.1.3) are very used industrial enzymes but presents drawbacks such as lack of stability, and poor recyclability. Most of these obstacles can be solved by lipase immobilization. The objective of this work was evaluated to magnetic magnesium spinel
Wee-Sim Choo et al.
Lipids, 44(2), 145-152 (2008-10-16)
Lipase-catalyzed transesterification of triolein with cinnamic and ferulic acids using an immobilized lipase from Candida antarctica (E.C. 3.1.1.3) was conducted to evaluate the antioxidant activity of the lipophilized products as model systems for enhanced protection of unsaturated oil. The lipophilized
M D Yago et al.
The British journal of nutrition, 78(1), 27-39 (1997-07-01)
The aim of the present study was to investigate in human subjects whether or not the ingestion of two liquid meals that differed only in their fatty acid composition (due to the addition of olive oil (group O) or sunflowerseed
R C Davis et al.
Genomics, 11(4), 1164-1166 (1991-12-01)
Human pancreatic lipase (EC 3.1.1.3) is a 56-kDa protein secreted by the acinar pancreas and is essential for the hydrolysis and absorption of long-chain triglyceride fatty acids in the intestine. In vivo, the 12-kDa protein cofactor, colipase, is required to
Louis Hermo et al.
Molecular reproduction and development, 75(4), 565-577 (2007-09-22)
Hormone-sensitive lipase (HSL, Lipe, E.C.3.1.1.3) functions as a triglyceride and cholesteryl esterase, supplying fatty acids, and cholesterol to cells. Gene-targeted HSL-deficient (HSL(-/-)) mice reveal abnormal spermatids and are infertile at 24 weeks after birth. The purpose of this study was
Rashmi Shakya et al.
Sexual plant reproduction, 23(2), 163-172 (2010-05-22)
Spatial distribution and compositional analyses of the lipidic constituents in pollen and stigma of sunflower (Helianthus annuus L. cv. Morden) were conducted using ultrastructural, histochemical, and biochemical analysis. Detection of secretions at the base of stigmatic papillae and neutral lipid
M Holmquist et al.
Lipids, 29(9), 599-603 (1994-09-01)
To determine whether Trp89 located in the lid of the lipase (EC 3.1.1.3) from Humicola lanuginosa is important for the catalytic property of the enzyme, site-directed mutagenesis at Trp89 was carried out. The kinetic properties of wild type and mutated
Daniel J Ericsson et al.
Journal of molecular biology, 376(1), 109-119 (2007-12-25)
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty acids. Under the appropriate conditions, the reaction is reversible, and so biotechnological applications commonly make use of their capacity for esterification as well as for
P Degn et al.
Carbohydrate research, 329(1), 57-63 (2000-11-22)
Glucose and maltose esters were synthesised in organic media by employing a lipase (E.C. 3.1.1.3) from Candida antarctica. In a second reaction step, a transglycosylation catalysed by a cyclodextrin glycosyltransferase (E.C. 2.4.1.19) from either Paenibacillus sp. F8 or Bacillus sp.
N Bitou et al.
Lipids, 34(5), 441-445 (1999-06-24)
The possible presence of an inhibitor of pancreatic lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was screened in 54 marine algae. An active inhibitor, caulerpenyne, was purified from an extract of Caulerpa taxifolia, using ethyl acetate extraction, followed by successive chromatographies on
Shu Pei Wang et al.
Endocrinology, 155(8), 3047-3053 (2014-05-07)
In male mice, deficiency of hormone sensitive lipase (HSL, Lipe gene, E.C.3.1.1.3) causes deficient spermatogenesis, azoospermia, and infertility. Postmeiotic germ cells express a specific HSL isoform that includes a 313 amino acid N-terminus encoded by a testis-specific exon (exon T1).
E Bohn et al.
FEBS letters, 296(3), 237-240 (1992-01-27)
A member of the annexin family (the heterotetrameric annexin II2p11(2) complex purified from porcine intestinal epithelium) was tested for its ability to affect different calcium-dependent intrinsic lipolytic activities of rat liver hepatic lipase (HL). Whereas annexin II in the presence
A Telefoncu et al.
Applied biochemistry and biotechnology, 26(3), 311-317 (1990-12-01)
Pancreatic lipase (EC 3.1.1.3) was immobilized by entrapping in a commercial preparation of acrylic/methacrylic acid ester-based copolymer (Eudragit E 30 D). The activity of the immobilized lipase beads with a diameter of 1.5-2.0 mm was found to be lower than
R Soliva-Fortuny et al.
Journal of dairy science, 89(11), 4096-4104 (2006-10-13)
The inactivation kinetics of a lipase from Pseudomonas fluorescens (EC 3.1.1.3.) were studied in a simulated skim milk ultrafiltrate treated with high-intensity pulsed electric fields. Samples were subjected to electric field intensities ranging from 16.4 to 27.4 kV/cm for up
S P Wang et al.
Obesity research, 9(2), 119-128 (2001-04-24)
To directly ascertain the physiological roles in adipocytes of hormone-sensitive lipase (HSL; E.C. 3.1.1.3), a multifunctional hydrolase that can mediate triacylglycerol cleavage in adipocytes. We performed constitutive gene targeting of the mouse HSL gene (Lipe), subsequently studied the adipose tissue
Paul Ramos et al.
Biochemistry, 42(43), 12488-12496 (2003-10-29)
Human pancreatic lipase (HPL, triacylglycerol acylhydrolase, EC 3.1.1.3) is a carboxyl esterase which hydrolyzes insoluble emulsified triglycerides and is essential for the efficient digestion of dietary fats. Though the three-dimensional structure of this enzyme has been determined, monitoring the conformational
S Chung et al.
Endocrinology, 142(10), 4272-4281 (2001-09-21)
The 84-kDa hormone-sensitive lipase (gene designation Lipe; EC 3.1.1.3) is a cholesterol esterase and triglyceride hydrolase that functions in the release of fatty acids from adipocytes. The role of hormone-sensitive lipase in other tissues such as the testis, where a
M Y Timmermans et al.
The Biochemical journal, 314 ( Pt 3), 931-936 (1996-03-15)
Pregastric esterase (PGE) (EC 3.1.1.3) was purified to homogeneity from calf pharyngeal tissue. The enzyme had an apparent molecular mass of 50 kDa, as determined by SDS/PAGE. The serine-binding reagent diethyl p-nitrophenyl phosphate was a potent inhibitor of PGE. This
M M Maia et al.
Bioresource technology, 76(1), 23-27 (2001-04-24)
Lipase (Glycerol ester hydrolase EC 3.1.1.3.) from a Brazilian strain of Fusarium solani FSI has been investigated. The effect of different carbon sources and trace elements added to basal medium was observed with the aim of improving enzyme production. Lipase
Benjamin Stauch et al.
Journal of lipid research, 56(12), 2348-2358 (2015-10-09)
Lipases (EC 3.1.1.3) are ubiquitous hydrolases for the carboxyl ester bond of water-insoluble substrates, such as triacylglycerols, phospholipids, and other insoluble substrates, acting in aqueous as well as in low-water media, thus being of considerable physiological significance with high interest
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