• Food Science of Animal Resources
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• v.40 no.1
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• pp.87-95
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• 2020

In this study, we separated and purified lipase inhibitory peptide from fermented milk by Lactobacillus plantarum Q180 with the aim of developing a new functional anti-lipase activity yogurt product. L. plantarum 180 was inoculated into 10% reconstituted skimmed milk and incubated at 37℃ until the pH of the culture reached pH 4.4. The lipase activity was measured using porcine pancreatic lipase. The lipase inhibitory peptides were gradually isolated by ultrafiltration, reversed phase column chromatography (RPC), reversed phase high-performance liquid chromatography (RP-HPLC), and gel permeation high-performance liquid chromatography (GP-HPLC) from the fermented milk by L. plantarum Q180. An ODS-AQ column was used for the RPC, a Vydac C18 column for the RP-HPLC, and a Superdex Peptide HR column for the GP-HPLC. The peptide was composed of Asp, Thr, Ile, Ser, Ala, and Gln, and the anti-lipase activity (IC₅₀) was 2,817 ㎍/mL.

• Korean Journal of Food Science and Technology
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• v.17 no.2
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• pp.60-64
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• 1985

To utilize microbial lipases for hydrolysis of milk fat, optimum reaction conditions and characteristics of enzymatic reactions of lipases originated from Rhizopus delemar, Mucor sp., and Candida cylindracea were investigated. Optimum pH and temperature were pH 5.6 and $45^{\circ}C$ for Rhizopus delemar lipase, pH7.5 and $35^{\circ}C$ for Mucor sp. lipase, and pH7.5 and $35^{\circ}C$ for Candida cylindracea lipase. Optimum lipase concentration and optimum substrate concentration were $600{\sim}800\;units/ml$ and 20% milk fat, regardless of their origin. Km values were 6.06% milk fat for Rhizopus delemar lipase, 7.69% for Mucor sp. lipase and 7.99% for Candida cylindracea lipase. Rate of lipid hydrolysis was Rhizopus delemar lipase>Mucor sp. lipase>Candida cylindracea lipase. As the reaction time was extended, liberation of short chain fatty acids was increased. After 8 hours reaction, capric acid content significantly increased with Candida cylindracea lipase, palmitic acid with Mucor sp. lipase and butyric acid with Rhizopus delemar lipase.

• Korean Journal of Food Science and Technology
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• v.20 no.6
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• pp.762-768
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• 1988

The lipolytic enzyme of milk from hormone treated and non treated cows was isolated and purified, It was shown that the crude lipase extract from the milk before and after a hormone treatment of the cows was different in color, foaming properties, yield and specific activity. Final purification of the lipase system was achieved by affinity chromatography on Heparin-Sepharose CL-6B. The lipase bound by Heparin-Sepharose was then characterised. The pH-optimum of the purified enzyme was 8.5 for butteroil emulsion as a substrate and the optimum temperature was $30^{\circ}C$ respectively. The molecular weight. determined by SDS-polyacrylamidegel electrophoresis, was about 70,000. The activity increased by 10% hen 0.01% bovine serum albumin was added to the substrate. The results indicate the enzymes obtained by affinity chromatography from milk before and after hormone treatment had the similar characteristics. The second lipolytic active component that was not bound by Heparin-Sepharose must be the cause of spontaneous rancidity.

• Food Science of Animal Resources
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• v.20 no.2
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• pp.101-106
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• 2000

Effects of Ph on the activity of lipase isolated from milk fat globules were investigated, using coconut oil and homogenized milk as substrate. With buttermilk as an enzyme source for coconut oil and homogenized milk substrates bell-shaped curve was observed at $37^{\circ}C$, having the highest activity at pH 9.5. However, lipase activity at $0^{\circ}C$ continuously increased up to pH 10.0. With the purified lipase for homogenized milk substrate, the bell -shaped curve and the highest activity were observed at $37^{\circ}C$ and pH 9.0, respectively. Lipase activity at $0^{\circ}C$ increased up to pH 10.0. The addition of bovine serum albumin to the coconut oil shifted the optimum pH to pH 9.5 and the activity remarkably declined at pH 10.0. The effect of pH on the stability of purified lipase was depending on the temperature. Wehn the lipase kept at $37^{\circ}C$ for 20 minutes, it's activity remarkably declined as pH increased: the activity at pH 10.0 was declined by 13% of that pH 8.5. However, when the lipase kept at $4^{\circ}C$ for 60minutes, the activity was stable within the range of pH 7.5 to 10.0.

• Journal of Animal Science and Technology
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• v.50 no.1
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• pp.111-120
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• 2008

The average milk fat content in goat milk was 3.88% on yearly basis. The milk fat content of 3.8% during summer season was lower than 4.2% during winter season. Total solid content increased in proportion to milk fat. When goat milk was stored at 4℃ for 24 hr, short-chain FFA(C4:0~C10:0) and medium- and long-chain FFA(C12:0~C18:1) increased about 106% and 203%, respectively. Induced lipolysis of goat milk by homogenization increased short-chain FFA and medium- and long-chain FFA by 22% and 199%. When goat milk was treated with calf lipase, there was increase of short-chain FFA by 9 times greater than increase of medium- and long-chain FFA by 5.6 times. Treatment with lipases from Candida rugosa and Pseudomonas fluorescens resulted in increase of medium- and long-chain FFA by 34 and 162 times, respectively, which was greater than increase of short-chain FFA by 6 and 14 times, respectively. Lipolysis in goat milk stored at 4℃ for 24 hr was correlated with LPL activity in goat milk(r=0.5635). Off-flavor of goat milk was correlated with LPL activity(r=0.5777). Milk fat content was negatively correlated with LPL activity(r=－0.4627). Palmitic acid content in goat milk was correlated with off-flavor(r=0.7226).

• Food Science of Animal Resources
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• v.34 no.6
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• pp.836-843
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• 2014

Obesity, a condition in which an abnormally large amount of fat is stored in adipose tissue, causing an increase in body weight, has become a major public health concern worldwide. The purpose of this study was to optimize the process for fermented milk for the production of a functional product with an anti-obesity effect by using Lactobacillus plantarum Q180 isolated from human feces. We used a 3-factor, 3-level central composite design (CCD) combined with the response surface methodology (RSM). Concentration of skim milk powder (%, $X_1$), incubation temperature ($^{\circ}C$, $X_2$), and incubation time (h, $X_3$) were used as the independent factors, whereas pH (pH, $Y_1$), anti-lipase activity (%, $Y_2$) and anti-adipogenetic activity (%, $Y_3$) were used as the dependent factors. The optimal conditions of fermented milk for the highest anti-lipase and anti-adipogenetic activity with pH 4.4 were the 9.5% of skim milk powder, $37^{\circ}C$ of incubation temperature, 28 h of incubation time. In the fermentation condition, the predicted values of pH, anti-lipase activity and anti-adipogenetic activity were 4.47, 55.55, and 20.48%, respectively. However, the actual values of pH, anti-lipase activity and anti-adipogenetic activity were 4.50, 52.86, and 19.25%, respectively. These results demonstrate that 9.5% of skim milk powder and incubation at $37^{\circ}C$ for 28 h were the optimum conditions for producing functional fermented milk with an anti-obesity effect.

• Korean Journal of Food Science and Technology
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• v.17 no.2
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• pp.75-80
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• 1985

To utilize lipase obtained from Candida cylindracea for lipid hydrolysis, methods to immobilize lipase by adsorption and reaction characteristics of the immobilized lipase by adsorption were investigated. Among the tested adsorbents, silica gel was selected as a suitable adsorbent. The optimum condition for adsorption of lipase was when 47.5 units of lipase were adsorbed to 1.6g of silica gel at pH7.0 and $5^{\circ}C$ for 100 min. Optimum pH and temperature for activity of the immobilized lipase were at $37^{\circ}C$ and pH7.0, which were same as the soluble lipase. Optimum enzyme concentration of the immobilized lipase were 30g for milk fat and 80g for olive oil, whereas those of the soluble lipase were 800 units for milk fat and 1200 units for olive oil. The optimum substrate concentrations of the immobilized and soluble lipases were 20% lipid, regardless of lipid types. Rapid hydrolysis of milk fat was observed with the soluble lipase for the initial 4 hours and with the immobilized lipase for the initial 8 hours. The immobilized lipase produced same amount of capric acid as the soluble lipase, but more myristic acid and less butyric acid than the soluble lipase.

• Journal of Dairy Science and Biotechnology
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• v.36 no.1
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• pp.49-71
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• 2018

Heat treatment is the most popular processing technique in the dairy industry. Its main purpose is to destroy the pathogenic and spoilage bacteria in order to ensure that the milk is safe throughout its shelf life. The protease and lipase that are present in raw milk might reduce the quality of milk. Plasmin and protease, which are produced by psychrotrophic bacteria, are recognized as the main causes of the deterioration in milk flavor and taste during storage. The enzymes in raw milk can be inactivated by heat treatment. However, the temperature of inactivation varies according to the type of enzyme. For example, some Pseudomonas spp. produce heat-resistant proteolytic and lipolytic enzymes that may not be fully inactivated by the low temperature and long time (LTLT) treatment. These types of enzymes are inhibited only by the high temperature and short time (HTST) or ultra-high temperature (UHT) treatment of milk.

• Applied Biological Chemistry
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• v.20 no.1
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• pp.101-104
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• 1977

Lipase from Geotrichum candidum was heat inactivated in 0.1M phosphate buffer solution. The thermal inactivation followed first order kinetics for the range of temperatures $50^{\circ}-80^{\circ}C$ except at $50^{\circ}C$. The changes in enthalpy, entropy and Gibbs free energy at $60^{\circ}C$ were 120.4 kJ/mol, 73.0 J/mol K and 96.9 kJ/mol respectively a value of $19^{\circ}C$(Geotrichum candidum lipase) is greater than that of lipases from milk and pancreas. The effect of detergents, lecithin and linoleic acid or the thermal inactivation of lipase was found to be negligible.

• The Korean Journal of Food And Nutrition
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• v.8 no.3
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• pp.192-198
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• 1995

For the production of EMC, various professes and lipases were used to hydrolyse cheese sulk. The optimal conditions of various proteases were as follows, pronase-3$0^{\circ}C$, p14 7.0, pancreatln-4$0^{\circ}C$, pH 8.0, pacific protease-3$0^{\circ}C$, pH 7.0 and protease from Asp. sp. -5$0^{\circ}C$, pH 8.0. The optimal conditions of various lipases were as follows ; pancreatic lipase-5$0^{\circ}C$, pH 8.0, palatase ML-5$0^{\circ}C$, pH 7.0 and lipase form Candida -4$0^{\circ}C$, pH U.0. After hydrolysation under optimal conditions, the amounts of free amino acid and free fatty ac14 were increased with reaction time. Hydrolysates of pacific protease and pronase were showed high amount of free amino acid(0.67mg/ml and 0.74mg/ml). Especially EMC had high amount of glutamic acid and leucine. Lipase from Candida cylindracea produced high amount of free fatty acid (24.63 mg/ml) Butyric acrid, palmitic acid, stearic acid and oleic acid among free fatty acids were showed high amounts. Sensory evaluation of various MC were tasted nth 8 panelist. EMC produced with pancreatic lipase was most bitterness and EMC produced with palatase ML was best acceptable cheese flavor.