• Journal of the Korean Society of Clothing and Textiles
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• v.32 no.6
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• pp.911-917
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• 2008

In this study, we reported the effect of porcine pancreas lipase treatment in the presence of a calcium chloride and Triton X-100 on moisture regain and wettability of PET fabrics. The moisture regain of PET fabrics in the presence of 0.5% surfactant showed a 1.5-fold decrease, compared to the absence of it. Triton X-100 acted as an inhibitor to porcine pancreas lipase hydrolytic activity. The moisture regain and wettability of porcine pancreas lipase treated PET fabrics improved when more than 10mM of calcium chloride was added to the treatment solution. Porcine pancreas lipase treatment caused voids and cracks on PET fabrics.

• Journal of the Korean Society of Clothing and Textiles
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• v.35 no.6
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• pp.670-677
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• 2011

This study is to optimize the enzymatic processing conditions of Polylactic Acid (PLA) fiber using lipase from Porcine pancreas as an environmental technology. Hydrolytic activity dependent on pH, temperature, enzyme concentration, and treatment time, and structural change of PLA fiber were evaluated. The PLA fiber hydrolysis by lipase was maximized at 50% (o.w.f) lipase concentration $50^{\circ}C$ for 120 minutes under pH 8.5. There was a change of the protein absorbance in the treatment solution before and after the lipase treatment. In addition, there was no substantial change in the molecular and crystalline structures of PLA by lipase treatment as confirmed by DSC, XRD, and FT-IR.

• Fisheries and Aquatic Sciences
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• v.12 no.1
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• pp.16-23
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• 2009

Lipids were extracted from marine rotifer, Brachionus rotundiformis in order to examine the functionality of lipid enzymatic modification. The fatty acids, palmitic, linoleic, oleic and stearic acids were the dominant forms accounting for approximately 35.8%, 21.5%, 15.9% and 7.7% of the total lipid content, respectively. Lipid fractions were categorized as neutral lipids (38.5%), glycolipids (45.9%) and phospholipids (17.6%), and after extraction from the rotifer were isolated by thin-layer chromatography (TLC) as free fatty acids (FFA), monoacylglycerol (MAG), diacylglycerol (DAG) and triacylglycerol (TAG). The production of polyunsaturated fatty acid (PUFA) concentrate from rotifer lipids was studied using lipase-catalyzed hydrolysis. In addition, rotifer lipids were modified by hydrolysis using lipases such as porcine pancreas, Candida rugosa and Rhizomucor miehei. The lipase from Rhizomucor miehei was effective in extracting linoleic acid (C 18:2), while the lipase from Candida rugosa was effective in palmitic acid (C16:0) extraction.

• Bulletin of the Korean Chemical Society
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• v.33 no.2
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• pp.409-414
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• 2012

Xanthorrhizol is a bisabolane type of natural sesquiterpene, the major component of essential oils of Curcuma xanthorrhiza. 2-(3-Methoxy-4-methylphenyl)propan-1-ol and 2-(3-hydroxy-4-methyl phenyl)propan-1-ol could be essential building block for enantioselective synthesis of xanthorrhizol. Enantioselective (c = 53%, E = $80{\pm}3$) for R-(+)-2-(3-hydroxy-4-methylphenyl) propan-1-ol and (c = 58%, E = $27{\pm}1$) for R-(+)-2-(3-methoxy-4-methylphenyl) propan-1-ol resolution processes were developed via lipase-catalyzed reaction. We found lipase Aspergillus oryzae (AOL) and Porcine pancreas (PPL) are selective to transesterification and hydrolysis in organic and aqueous phase. Modified demethylated substrate is appropriate for enantioselective hydrolysis reaction without any additives. Enantiopure chiral alcohol was crystallized from ethyl acetate/n-hexane co-solvent system. Gram scale resolved chiral intermediate will facilitate the synthesis of the unnatural S-(+)-xanthorrhizol, the corresponding isomer of the natural one.

• Journal of the Korean Society of Clothing and Textiles
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• v.36 no.6
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• pp.653-662
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• 2012

This study measured the effect of general pre-treatment on PLA fabrics to confirm the benefits of enzymatic processing on PLA fabrics in the textile industry as well as evaluated the hydrolytic activities of three lipases. The effects of lipase hydrolysis were analyzed through moisture regain, dyeing ability, tensile strength, and surface morphology. As a result, PLA fibers were easily damaged by a low concentration of sodium hydroxide and a low treatment temperature. The optimal treatment conditions of Lipase from Candida cylindracea were pH 8.0, $40^{\circ}C$, and 1,000 U. The optimal treatment conditions for Lipase from Candida rugosa were pH 7.2, $37^{\circ}C$, and 1,000 U. The optimal treatment conditions for Lipase from Porcine pancreas were pH 8.0, $37^{\circ}C$, and 2,000 U. The moisture regain and dyeing ability of PLA fabrics increased and the tensile strength of PLA fabrics decreased. The results of surface morphology revealed that there were some cracks due to hydrolysis on the surface of the fiber.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.12 no.1
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• pp.276-280
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• 2011

This study investigated the activation conditions of pancreatic enzymes from porcine pancreas. Duodenum induced the activation of pancreatic protease and lipase in pancreas. When 10% duodenum was added to pancreatic juice and the mixture was incubated at $30^{\circ}C$ for 90 min or at $25^{\circ}C$ for 4 hrs, the activities of pancreatic protese and lipase reached the peak. When the pancreatin was prepared by sequential process of enzymatic activation at $25^{\circ}C$ for 4 hrs, centrifugation, acetone precipitation and freeze-drying, the specific activities of pancreatic protease, lipase and amylase were 136, 116 and 400 U/mg-protein, respectively. The protease, lipase and amylase activities of the prepared pancreatin were 5.4, 58.0 and 16.0 times higher than those of USP standard, respectively.

• Microbiology and Biotechnology Letters
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• v.36 no.4
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• pp.299-306
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• 2008

Human pancreatic lipase is a digestive enzyme which is synthesized in pancreas, secreted into small intestine, and there hydrolyze the fat in food. Pancreatic lipase protein composes of catalytic domain and colipase-binding domain. In this research, the gene segments corresponding to total protein, catalytic domain, and co lipase-binding domain were cloned by PCR method, inserted into an expression vector, and then used to transform Escherichia coli BL21 (DE3). The recombinant proteins produced were purified and injected intramuscularly three times into laying hens. The egg yolk antibodies (IgY) were obtained from the egg yolks and tested for their antibody titer. Among three IgY, the IgY against colipase-binding domain showed the highest antibody titer. All three IgY had inhibitory effects on the porcine pancreatic lipase. Among them, the IgY against colipase-binding domain showed the highest inhibition effects. The fat diet with corn oil and IgY was administrated to the experimental rats and their blood compositions were examined with time course. The triglyceride concentration of treated rats was decrease meaningfully when compared with those of control rats. This suggested that the IgY against colipase-binding domain antigen inhibited pancreatic lipase in vivo.

• Journal of Dairy Science and Biotechnology
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• v.7 no.1
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• pp.6-19
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• 1989

Twenty-five commercial food grade and alalytical grade lipases were used to study the patterns of release of short-chain free fatty acids (FFA) from milk fat in cheese slurries. Principal component Analysis showed that there were four distinctive groups by the FFA ratios and five groups by the FFA concentrations. However, Average Linkage Cluster Analysis showed that the patterns of FFA released were dependent upon distance defined between groups of lipases. All the lipases tested with both statistical analysis had distinctive specificities in hydrolyzing short-chain FFA from milk fat. Lipases from ruminant-animal origins produced an extremely high ratio (>40%) of butyric acid and a low ratio (<26%) of capric acid to total short chain FFA. Lipases from porcinepancreas and some microbial origins showed balanced production in both bytyric and capric acid. However, most lipases from microbial origins released a high ratio of capric acid but similar ratios to other origin enzymes for short-chain free fatty acids. Ruminant-animal origin lipases produced short-chain FFA much higher in concentration than other lipases. Lipases from porcine pancreas as well as microbial origins showed different concentrations of the fatty acids. Ratios of short-chain FFA in each sample were not significantly changed during incubation periods (4 wk), whereas concentrations of the FFA increased considerably.