• Microbiology and Biotechnology Letters
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• v.23 no.5
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• pp.526-530
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• 1995

Phospholipase A$_{2}$ (PLA$_{2}$) is lipolytic enzyme that has known to be involved in inflammation. In the course of our screening for antiinflammatory compounds from natural products, a compound having PLA$_{2}$ inhibitory activities was isolated from the methanol extract of Umbilicaria esculenta. The compound was identified as lecanoric acid based on various NMR studies including DEPT, HETERO-COSY and HMBC experiments. Lecanoric acid inhibited human rheumatoid synovial PLA$_{2}$ activity with IC$_{50}$ of 0.17 mM and also exhibited antitumor activity (ED$_{50}$=2.7 $\mu $g/ml) against skin tumor cell line (LOX-IMVI).

• BMB Reports
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• v.45 no.1
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• pp.14-19
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• 2012

A feruloyl esterase encoding gene (designated fae6), derived from a leachate metagenomic library, was cloned and the nucleotide sequence of the insert DNA determined. Translational analysis revealed that fae6 consists of a 515 amino acid poly-peptide, encoding a 55 kDa pre-protein. The Fae6 primary structure contained the G-E-S-A-G sequence, which corresponds well with a typical catalytic serine sequence motif (G-x-S-x-G). The fae6 gene was successfully over-expressed in E. coli and the recombinant protein was purified to 8.4 fold enrichment with 17% recovery. The $K_M$ data showed Fae6 has a high affinity to methyl sinapate while thermostability data indicated that fae6 was thermolabile with a half life ($T_{1/2}$) < 30 min at $50^{\circ}C$. High affinity for Fae6 against methyl sinapate, methyl ferulate and ethyl ferulate suggest that the enzyme can be useful in hydrolyzing ferulated polysaccharides in a biorefinery process.

• Journal of Microbiology
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• v.41 no.1
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• pp.22-27
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• 2003

A lipase from Aeromonas sp. LPB 4, a psychrotophile isolated from a sea sediment was purified and characterized. The lipase was purified 53.5 fold to a homogeneous state by acetone precipitation and QAE sephadex column chromatography and its molecular weight was determined to be 50 kDa by SDS-PAGE. The enzyme exhibited maximum activity at 10$^{\circ}C$ and was stable at temperatures lower than 50$^{\circ}C$. This lipase favored substrates containing medium carbon chain of acyl group, while too low and high carbon chain decreased its activity. The lipolytic activity of purified lipase was slightly increased by the addition of 0.1% detergent, but decreased by 1% of detergent. Butanol severely decreased the lipase activity while methanol increased the activity about 15%.

• Journal of the Korean Society of Food Science and Nutrition
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• v.41 no.12
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• pp.1708-1715
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• 2012

The purpose of this study was to investigate whether water extracts of Sparassis crispa (SC) have anti-obesity effects. Treatment of mature adipocytes with SC caused a decrease in lipid accumulation (assessed by Oil Red O staining) and an increase in glycerol release. Mice were induced to obesity by a high fat diet (45% fat in total kcal) and experimental groups were treated with two different dosages of SC extracts, a low SC (LSC, 100 mg/kg/day) or high SC (HSC, 300 mg/kg/day). SC extracts were administered by gavages for 10 weeks in the experimental groups, while the control group was fed with distilled water. The body weight gain of mice fed SC was significantly reduced (11.88% lower in LSC, 14.54% lower in HSC) compared to the control group. Additionally, there were significantly reduced serum levels of triglycerides (13.57% lower in LSC, 19.46% lower in HSC), total cholesterol (32.22% lower in LSC, 24.67% lower in HSC) and glucose (28.85% lower in LSC, 25.82% lower in HSC) in mice fed SC compared to the control group. Hepatic triglycerides in mice fed SC were lower (9.68% lower in LSC, 14.24% lower in HSC) than the control group and total cholesterol levels were also lower in mice fed SC (38.72% lower in LSC, 35.20% in HSC). These results demonstrate that the water extract of SC may enhance lipolysis and up-regulate the expression of lipolytic enzymes in vitro and reduce body weight in vivo. These significant effects were found for both low and high doses of SC treatment, and suggest SC can be used as potential therapeutic substances for the prevention and treatment of obesity.

• Food Science of Animal Resources
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• v.33 no.6
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• pp.772-780
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• 2013

The aim of this study was to investigate the effect of season and location on activities of enzyme produced by psychrotrophic bacteria isolated from raw milk located in Kyunggi region of South Korea. Agar diffusion and colorimetric methods were used for the lipase and protease activities of psychrotrophic bacteria. Intensities of dark blue and transparent ring around colony were compared for activity measurement. Nutrient agar with 1% skim milk added was employed for measuing protease activity. 14 strains of Arthrobacter russicus with lipase activity and 19 strains of Chryserobacterium shigense with protease activities were found to be present. It was found that Acinetobacter genomospecies 10 (match %: 99.90) isolated from B region in fall was the most lipolytic species, whereas Serratia liquefaciens (match %: 99.39) isolated from the same region in spring was the most proteolytic species. Growth curve of Acinetobacte and Serratia liquefaciens was a typical sigmoidal form. Lipase activity increased with incubation time, but its activity began to drop at stationary to motality phase. Optimum condition for incubation time, pH and temperature for extracellular lipase from Acinetobacter genomospecies 10 (match %: 99.90) was 12 h, 8.5, and $45^{\circ}C$, respectively. Extracellular protease from Serratia liquefaciens (match %:99.39) had the same optimum incubation time and pH as extracellular lipase, but optimum temperature was $35^{\circ}C$.

• Proceedings of the Ginseng society Conference
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• 1990.06a
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• pp.15-19
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• 1990

We have been isolating various physiologically active substances from non-saponin fraction of Korean Red Ginseng These are adenosine, gyro-glutamic acid, dencichine and acidic polysaccharide. Adenosine and gyro-glutamic acid are loom to inhibit epinephrine-induced lipolysis in fat cells and stimulate the insulin-mediated lipogenesis. In addition to these actions, adenosine was found to inhibit both norepinephrine- and histamine-induced aorta constriction, and pyre·glutamic acid inhibits angiotensin-converting enzyme. Dencichine stimulated histamine-induced aorta constriction. Finally, acidic polysaccharide was found to inhibit both lipolytic and anorexigenic actions of Toxohormone-L. Based on these experimental results, I presented a brief review on these compounds isolated from non- saponin fraction of Korea Red Ginseng. Keywords Panax ginseng, Korean red ginseng, adenosine, pyroglutamic acid, dencichine, acidic polysac- charide, lipolysis, lipogenesis, angiotensin-converting enzyme, toxohormone-L.

• Microbiology and Biotechnology Letters
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• v.46 no.3
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• pp.234-243
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• 2018

The Antarctic Ocean contains numerous microorganisms that produce novel biocatalysts that can have applications in various industries. We screened various psychrophilic bacterial strains isolated from the Ross Sea and found that a Croceibacter atlanticus strain (Stock No. 40-F12) showed high lipolytic activity on a tributyrin plate. We isolated the corresponding lipase gene (lipCA) by shotgun cloning and expressed the LipCA enzyme in Escherichia coli cells. Homology modeling of LipCA was carried out using the Spain Arreo lake metagenome alpha/beta hydrolase as a template. According to the model, LipCA has an ${\alpha}/{\beta}$ hydrolase fold, Gly-X-Ser-X-Glymotif, and lid sequence, indicating that LipCA is a typical lipase enzyme. Active LipCA enzyme was purified fromthe cell-free extract by ammonium sulfate precipitation and gel filtration chromatography. We determined its enzymatic properties including optimum temperature and pH, stability, substrate specificity, and organic solvent stability. LipCA was immobilized by the cross-linked enzyme aggregate (CLEA) method and its enzymatic properties were compared to those of free LipCA. After cross-linking, temperature, pH, and organic solvent stability increased considerably, whereas substrate specificities did not changed. The LipCA CLEA was recovered by centrifugation and showed approximately 40% activity after 4th recovery. This is the first report of the expression, characterization, and immobilization of a C. atlanticus lipase, and this lipase could have potential industrial application.

• Journal of Animal Science and Technology
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• v.55 no.4
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• pp.303-314
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• 2013

Knowledge regarding lipid catabolism has been of great interest in the field of animal sciences. In the livestock industry, excess fat accretion in meat is costly to the producer and undesirable to the consumer. However, intramuscular fat (marbling) is desirable to enhance carcass and product quality. The manipulation of lipid content to meet the goals of animal production requires an understanding of the detailed mechanisms of lipid catabolism to help meticulously design nutritional, pharmacological, and physiological approaches to regulate fat accretion. The concept of a basic system of lipases and their co-regulators has been identified. The major lipases cleave triacylglycerol (TAG) stored in lipid droplets in a sequential manner. In adipose tissue, adipose triglyceride lipase (ATGL) performs the first and rate-limiting step of TAG breakdown through hydrolysis at the sn-1 position of TAG to release a non-esterified fatty acid (NEFA) and diacylglycerol (DAG). Subsequently, cleavage of DAG occurs via the rate-limiting enzyme hormone-sensitive lipase (HSL) for DAG catabolism, which is followed by monoglyceride lipase (MGL) for monoacylglycerol (MAG) hydrolysis. Recent identification of the co-activator (Comparative Gene Identification-58) and inhibitor [G(0)/G(1) Switch Gene 2] of ATGL have helped elucidate this important initial step of TAG breakdown, while also generating more questions. Additionally, the roles of these lipolysis-related enzymes in muscle, liver and skin tissue have also been found to be of great importance for the investigation of systemic lipolytic regulation.

• Journal of Microbiology and Biotechnology
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• v.32 no.11
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• pp.1390-1395
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• 2022

Acne is a chronic inflammatory disease of the sebaceous gland attached to the hair follicles. Cutibacterium acnes is a major cause of inflammation caused by acne. It is well known that C. acnes secretes a lipolytic enzyme to break down lipids in sebum, and free fatty acids produced at this time accelerate the inflammatory reaction. There are several drugs used to treat acne; however, each one has various side effects. According to previous studies, sulforaphene (SFEN) has several functions associated with lipid metabolism, brain function, and antibacterial and anti-inflammatory activities. In this study, we examined the effects of SFEN on bacterial growth and inflammatory cytokine production induced by C. acnes. The results revealed that SFEN reduced the growth of C. acnes and inhibited proinflammatory cytokines in C. acnes-treated HaCaT keratinocytes through inhibiting NF-κB-related pathways. In addition, SFEN regulated the expression level of IL-1α, a representative pro-inflammatory cytokine expressed in co-cultured HaCaT keratinocytes and THP-1 monocytes induced by C. acnes. In conclusion, SFEN showed antibacterial activity against C. acnes and controlled the inflammatory response on keratinocytes and monocytes. This finding means that SFEN has potential as both a cosmetic material for acne prevention and a pharmaceutical material for acne treatment.