scholarly journals Evaluation of the catalytic activity of lipases immobilized on chrysotile for esterification

2003 ◽  
Vol 75 (2) ◽  
pp. 157-162 ◽  
Author(s):  
Jane E. S. Silva ◽  
Paulo C. Jesus
Keyword(s):  
Catalytic Activity ◽  
Lauric Acid ◽  
Rhizopus Oryzae ◽  
Candida Rugosa ◽  
Magnesium Silicate ◽  
Pseudomonas Cepacia ◽  
Organic Media ◽  
Ester Synthesis ◽  
Mucor Javanicus ◽  
Different Sources

In the present work, the ester synthesis in organic media catalyzed by lipases immobilized on chrysotile was studied. Lipases of different sources (Mucor javanicus, Pseudomonas cepacia, Rhizopus oryzae, Aspergillus niger and Candida rugosa) were immobilized on chrysotile, an inexpensive magnesium silicate, and used for esterification of hexanoic, octanoic and lauric acid with methanol, ethanol, 1-butanol and 1-octanol at 25ºC in hexane as solvent. The best results were obtained with Mucor javanicus lipase and lauric acid giving yields of 62-97% of ester.

Application of an immobilized Rhizopus oryzae lipase to batch and continuous ester synthesis with a mixture of a lauric acid and fusel oil

2018 ◽  
Vol 119 ◽  
pp. 61-68 ◽  
Author(s):  
Renata N. Vilas Bôas ◽  
Annie A. Ceron ◽  
Heitor B.S. Bento ◽  
Heizir F. de Castro
Keyword(s):  
Lauric Acid ◽  
Rhizopus Oryzae ◽  
Ester Synthesis ◽  
Rhizopus Oryzae Lipase ◽  
Fusel Oil

Agarose-chymotrypsin as a catalyst for peptide and amino acid ester synthesis in organic media

1989 ◽  
Vol 11 (11) ◽  
pp. 811-816 ◽  
Author(s):  
Rosa M. Blanco ◽  
Jos� M. Guis�n ◽  
Peter J. Halling
Keyword(s):  
Amino Acid ◽  
Acid Ester ◽  
Amino Acid Ester ◽  
Organic Media ◽  
Ester Synthesis

Ultrathin Anionic Tungstophosphite Molecular Wire with Tunable Hydrophilicity and Catalytic Activity for Selective Epoxidation in Organic Media

2017 ◽  
Vol 23 (69) ◽  
pp. 17497-17503 ◽  
Author(s):  
Zhenxin Zhang ◽  
Masahiro Sadakane ◽  
Michikazu Hara ◽  
Wataru Ueda
Keyword(s):  
Catalytic Activity ◽  
Organic Media ◽  
Molecular Wire

scholarly journals Hydrolysis Activity of Virgin Coconut Oil Using Lipase from Different Sources

Scientifica ◽  
2018 ◽  
Vol 2018 ◽  
pp. 1-6 ◽  
Author(s):  
T. A. V. Nguyen ◽  
Truong D. Le ◽  
Hoa N. Phan ◽  
Lam B. Tran
Keyword(s):  
Time Course ◽  
Candida Rugosa ◽  
Coconut Oil ◽  
Virgin Coconut Oil ◽  
Porcine Pancreas ◽  
Hydrolysis Degree ◽  
Porcine Pancreas Lipase ◽  
Hydrolysis Process ◽  
Hydrolysis Of ◽  
Different Sources

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).

scholarly journals Highly Efficient Lipase Catalyzed Monoaminolysis Reaction of Diesters with Benzylamine

2019 ◽  
Vol 14 (6) ◽  
pp. 1934578X1985998
Author(s):  
Gerardo Valerio-Alfaro ◽  
Patricia Harumi Castillo-Carrasco ◽  
Olaya Pirene Castellanos Onorio ◽  
Jorge Bautista Naranjos
Keyword(s):  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Diethyl Malonate ◽  
Rhizomucor Miehei ◽  
Solvent Polarity ◽  
Pharmaceutical Products ◽  
Pseudomonas Cepacia ◽  
Butyl Ether ◽  
Highly Efficient ◽  
Diethyl Succinate

Preparation of amides by biocatalyzed aminolysis reactions has greatly increased because these processes play an important role in the preparation of some pharmaceutical products and their intermediates. A highly efficient synthesis of malonic (5), succinic (6), and malic (8) monoamide esters by desymmetrization transformations (mono aminolysis reactions) of their diesters is presented. The immobilized lipase from Candida antarctica (CaL-B, Novozym 435) catalyzed the mono aminolysis of bifunctional compounds: diesters such as diethyl malonate (1), diethyl succinate (2), and ( R, S)-malate (3), leading to their corresponding monoamides (5), (6), and (8), respectively, with high conversions after a 24 hour reaction in the presence of an organic solvent. Increasing the solvent polarity from toluene, methyl t-butyl ether to dioxane led to an improved conversion. According to qualitative and quantitative GC-MS analysis, conversions of diesters (1), (2), and (3) into their mono amide esters were in the range 65%-97%. CaL-B was the best biocatalyst of the commercial lipases used, including those from Candida rugosa, Rhizomucor miehei, Carica papaya, and Pseudomonas cepacia. Likewise, a yield of 91% regioisomeric, but virtually racemic ( R,S)-mono amide (8) was obtained as the single product in dioxane.

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