ChemInform Abstract: Regioselective Acetylation of 2-Aryl-2-butene-1,4-diols and Hydrolysis of Their Diacetates Using Porcine Pancreas Lipase.

Two types of lipase, Candida rugosa lipase (CRL) and porcine pancreas lipase (PPL), were used to hydrolyze virgin coconut oil (VCO). The hydrolysis process was carried out under four parameters, VCO to buffer ratio, lipase concentration, pH, and temperature, which have a significant effect on hydrolysis of lipase. CRL obtained the best hydrolysis condition at 1 : 5 of VCO to buffer ratio, 1.5% of CRL concentration, pH 7, and temperature of 40°C. Meanwhile, PPL gave different results at 1 : 4 of VCO to buffer ratio, 2% of lipase concentration, pH 7.5, and 40°C. The highest hydrolysis degree of CRL and PPL was obtained after 16 hours and 26 hours, reaching 79.64% and 27.94%, respectively. Besides, the hydrolysis process was controlled at different time course (every half an hour) at the first 4 hours of reaction to compare the initial hydrolysis degree of these two lipase types. FFAs from hydrolyzed products were isolated and determined the percentage of each fatty acid which contributes to the FFAs mixture. As a result, medium chain fatty acids (MCFAs) made up the main contribution in composition of FFAs and lauric acid (C12) was the largest segment (47.23% for CRL and 44.23% for PPL).

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Highly Regioselective Hydrolysis of Substituted 2-Benzylidene-1,3-propylene Diacetates Using Porcine Pancreas Lipase

Chemistry Letters ◽

10.1246/cl.2007.814 ◽

2007 ◽

Vol 36 (6) ◽

pp. 814-815 ◽

Cited By ~ 10

Author(s):

Tsuyoshi Miura ◽

Yuya Kawashima ◽

Satoe Umetsu ◽

Daisuke Kanamori ◽

Nanae Tsuyama ◽

...

Keyword(s):

Porcine Pancreas ◽

Porcine Pancreas Lipase ◽

Hydrolysis Of ◽

Regioselective Hydrolysis

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Stereoselectivity of lipases in supercritical carbon dioxide. I. Dependence of the regio- and enantioselectivity of porcine pancreas lipase on the water content during the hydrolysis of triolein and its partial glycerides

Chemistry and Physics of Lipids ◽

10.1016/0009-3084(95)02513-8 ◽

1996 ◽

Vol 79 (2) ◽

pp. 101-106 ◽

Cited By ~ 14

Author(s):

Gaby Glowacz ◽

Mirko Bariszlovich ◽

Michael Linke ◽

Peter Richter ◽

Cornelia Fuchs ◽

...

Keyword(s):

Carbon Dioxide ◽

Supercritical Carbon Dioxide ◽

Water Content ◽

Porcine Pancreas ◽

Partial Glycerides ◽

Porcine Pancreas Lipase ◽

Hydrolysis Of ◽

Supercritical Carbon

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Regioselective Acetylation of 2-Aryl-2-butene-1,4-diols and Hydrolysis of Their Diacetates Using Porcine Pancreas Lipase

Chemistry Letters ◽

10.1246/cl.2009.892 ◽

2009 ◽

Vol 38 (9) ◽

pp. 892-893 ◽

Cited By ~ 5

Author(s):

Naka Koyata ◽

Takuya Nagai ◽

Masashi Kawasaki ◽

Takuya Noguchi ◽

Masayuki Kirihara ◽

...

Keyword(s):

Porcine Pancreas ◽

Porcine Pancreas Lipase ◽

Hydrolysis Of

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Evaluation of Strategies to Produce Highly Porous Cross-Linked Aggregates of Porcine Pancreas Lipase with Magnetic Properties

Molecules ◽

10.3390/molecules23112993 ◽

2018 ◽

Vol 23 (11) ◽

pp. 2993 ◽

Cited By ~ 21

Author(s):

José Guimarães ◽

Raquel Giordano ◽

Roberto Fernandez-Lafuente ◽

Paulo Tardioli

Keyword(s):

Magnetic Nanoparticles ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Soy Protein ◽

Bovine Serum ◽

Amino Groups ◽

Porcine Pancreas ◽

Porcine Pancreas Lipase ◽

Hydrolysis Of ◽

Highly Porous

The preparation of highly porous magnetic crosslinked aggregates (pm-CLEA) of porcine pancreas lipase (PPL) is reported. Some strategies to improve the volumetric activity of the immobilized biocatalyst were evaluated, such as treatment of PPL with enzyme surface-modifying agents (polyethyleneimine or dodecyl aldehyde), co-aggregation with protein co-feeders (bovine serum albumin and/or soy protein), use of silica magnetic nanoparticles functionalized with amino groups (SMNPs) as separation aid, and starch as pore-making agent. The combination of enzyme surface modification with dodecyl aldehyde, co-aggregation with SMNPs and soy protein, in the presence of 0.8% starch (followed by hydrolysis of the starch with α-amylase), yielded CLEAs expressing high activity (immobilization yield around 100% and recovered activity around 80%), high effectiveness factor (approximately 65% of the equivalent free enzyme activity) and high stability at 40 °C and pH 8.0, i.e., PPL CLEAs co-aggregated with SMNPs/bovine serum albumin or SMNPs/soy protein retained 80% and 50% activity after 10 h incubation, respectively, while free PPL was fully inactivated after 2 h. Besides, highly porous magnetic CLEAs co-aggregated with soy protein and magnetic nanoparticles (pm-SP-CLEAs) showed good performance and reusability in the hydrolysis of tributyrin for five 4h-batches.

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Enzymatic hydrolysis of coconut oil using free and immobilized porcine pancreas lipases

Science and Technology Development Journal ◽

10.32508/stdj.v19i2.654 ◽

2016 ◽

Vol 19 (2) ◽

pp. 70-77

Author(s):

Van Thi Ai Nguyen ◽

Hoa Ngoc Phan ◽

Lam Bich Tran ◽

Ai Tran Diem Chau

Keyword(s):

Enzymatic Hydrolysis ◽

Coconut Oil ◽

Porcine Pancreas ◽

Hydrolysis Degree ◽

Immobilized Lipases ◽

Porcine Pancreas Lipase ◽

Hydrolysis Conditions ◽

First Time ◽

Hydrolysis Of ◽

Free Lipase

The aim of this study is to evaluate the effect of some factors on the hydrolysis of coconut oil (CO) in the present of two kind of enzymes, the free lipases and immobilized lipases porcine pancreas. The activities of these two lipases under the optimal hydrolysis conditions was determined. The effects of factors on hydrolysis degree of coconut oil was investigated: the ratio of enzyme to substrate, the pH condition, and the temperature. The best conditions for the high hydrolysis degree in case of using lipase from porcine pancreas ascatalyst included: the ratio of the enzyme to substrate of 90(U/mL), and the pH condition of 8.5 at the temperature of 40oC. The best reaction condition the case of using immobilized porcine pancreas lipase as the catalyst was determined, including: the ratio enzyme to substrate of 393U/g, the pH condition of 7.5 and the temperature of 35oC. The hydrolysis degree of CO by immobilized porcine pancreas lipase was increased slower than free lipase at the first time. The highest hydrolysis degree achieved with immobilized porcine pancreas and free porcine pancreas lipase was 72.26% and 68.61%, respectively.

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