Lipase from Burkholderia cepacia (Amano Lipase, ≥ 2200 U·g−1, pH 7.0, 50 °C) was purchased from Sigma Aldrich (Tokyo, Japan). The silane precursor tetraethoxysilane (TEOS) was supplied by Across Organic (Morris, NJ, USA) and used without further purification. Ethanol (99% pure), ammonia (28% pure), hydrochloric acid (36% pure) and arabic gum were obtained from Synth (São Paulo, Brazil). Water was purified by reverse osmosis and deionized through a Milli-Q four-cartridge organic-free water purification system. Olive (low acidity), sunflower, soybean, and colza oils were purchased at a local market. For covalent binding the bifunctional agents glutaraldehyde or epichlorohydrin from Sigma Aldrich were used. The protic ionic liquid N-methylmonoethanolamine pentanoate was supplied by the Federal University of Bahia (UFBA). Other chemicals were of analytical grade and used as purchased.
Amano lipase
Manufactured by Merck Group
Sourced in Japan
Amano Lipase is a commercial enzyme preparation derived from the fungus Aspergillus niger. It is a lipase enzyme that catalyzes the hydrolysis of fats and oils.
Automatically generated - may contain errors
Lab products found in correlation
Glutaraldehyde, by Merck Group (1 mentions)
Epichlorohydrin, by Merck Group (1 mentions)
Lysozyme, by Merck Group (1 mentions)
Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions)
Rabbit serum, by Thermo Fisher Scientific (1 mentions)
Lipase from aspergillus niger, by Merck Group (1 mentions)
Rhizomucor miehei lipase, by Novozymes (1 mentions)
Rhizopus oryzae lipase, by Merck Group (1 mentions)
Pseudomonas fluorescens lipase, by Merck Group (1 mentions)
Candida antarctica lipase type b, by Merck Group (1 mentions)
Esterase, by Merck Group (1 mentions)
Porcine pancreas lipase, by Merck Group (1 mentions)
Thermomyces lanuginosus lipase, by Merck Group (1 mentions)
Candida rugosa lipase, by Merck Group (1 mentions)
3 protocols using amano lipase
1
Lipase-Catalyzed Transesterification of Vegetable Oils
2
Hydrogel Weight Swelling in Biological Fluids
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Disk-shaped hydrogel samples (o.d.
4 mm, 3 mm in height) were synthesized using the previously mentioned
method. The initial weight of each hydrogel sample was measured, after
which they were immersed in different media, namely, PBS (Gibco 10010023),
Fetal bovine serum (Gibco, 26140079) Rabbit Serum (Gibco, 16120107)
and Human Serum. Human serum was prepared using Amano Lipase (0.005
mg/mL in PBS, Sigma-Aldrich, 534641) and Lysozyme (0.013 mg/mL in
PBS, Sigma-Aldrich, 62971). Three replicates were prepared for each
solution. Weight swelling ratios of the samples were calculated after
3 days according to where Wt is the
swollen weight of the hydrogels after 3 days inside the medium and Wi is the initial weight of the hydrogel.
4 mm, 3 mm in height) were synthesized using the previously mentioned
method. The initial weight of each hydrogel sample was measured, after
which they were immersed in different media, namely, PBS (Gibco 10010023),
Fetal bovine serum (Gibco, 26140079) Rabbit Serum (Gibco, 16120107)
and Human Serum. Human serum was prepared using Amano Lipase (0.005
mg/mL in PBS, Sigma-Aldrich, 534641) and Lysozyme (0.013 mg/mL in
PBS, Sigma-Aldrich, 62971). Three replicates were prepared for each
solution. Weight swelling ratios of the samples were calculated after
3 days according to where Wt is the
swollen weight of the hydrogels after 3 days inside the medium and Wi is the initial weight of the hydrogel.
3
Comparative Evaluation of Lipase Preparations
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Commercially available lipases were used as follows: (i) Immobilized lipases:
Candida antarctica lipase type B immobilized on acrylic resin (CAL-B, 7,300.0 U/g), Thermomyces lanuginosus lipase immobilized on immobead-150 (TLL, 250.0 U/g), Rhizopus oryzae lipase immobilized on immobead-150 (ROL, 340.0 U/g), Pseudomonas fluorescens lipase immobilized on immobead-150 (PFL, ≥ 600 U/g), Pseudomonas fluorescens lipase immobilized in Sol-Gel (AK, ≥ 30 U/g), Pseudomonas fluorescens lipase immobilized in Sol-Gel on pumice (AK, ≥ 8.0 U/g) and Amano lipase PS from Burkholderia cepacia immobilized on diatomaceous earth (PS-IM, ≥ 500 U/g) were acquired from Sigma-Aldrich®, Rhizomucor miehei lipase immobilized in anionic resin (RML, 150.0 U/g) was purchased from Novozymes ® . (ii) Unsupported lipase preparations: Pseudomonas fluorescens lipase (AK, 22,100.0 U/g), Penicillium camemberti lipase (G, 50.0 U/g), lipase from Rhizopus niveus (RNL, ≥ 1.5 U/mg), Amano lipase from Mucor javanicus (MJL, ≥ 10,000 U/g) and lipase from Aspergillus niger (ANL, 200 U/g) were acquired from Sigma-Aldrich ® . Porcine pancreas lipase (PPL, 46.0 U/g solid), and Candida rugosa lipase (CRL, 1.4 U/g) were obtained from Sigma-Aldrich ® . (iii) Esterase, immobilized in Eupergit ® C from hog liver (~200 U/g) was obtained from Sigma-Aldrich ® .
Candida antarctica lipase type B immobilized on acrylic resin (CAL-B, 7,300.0 U/g), Thermomyces lanuginosus lipase immobilized on immobead-150 (TLL, 250.0 U/g), Rhizopus oryzae lipase immobilized on immobead-150 (ROL, 340.0 U/g), Pseudomonas fluorescens lipase immobilized on immobead-150 (PFL, ≥ 600 U/g), Pseudomonas fluorescens lipase immobilized in Sol-Gel (AK, ≥ 30 U/g), Pseudomonas fluorescens lipase immobilized in Sol-Gel on pumice (AK, ≥ 8.0 U/g) and Amano lipase PS from Burkholderia cepacia immobilized on diatomaceous earth (PS-IM, ≥ 500 U/g) were acquired from Sigma-Aldrich®, Rhizomucor miehei lipase immobilized in anionic resin (RML, 150.0 U/g) was purchased from Novozymes ® . (ii) Unsupported lipase preparations: Pseudomonas fluorescens lipase (AK, 22,100.0 U/g), Penicillium camemberti lipase (G, 50.0 U/g), lipase from Rhizopus niveus (RNL, ≥ 1.5 U/mg), Amano lipase from Mucor javanicus (MJL, ≥ 10,000 U/g) and lipase from Aspergillus niger (ANL, 200 U/g) were acquired from Sigma-Aldrich ® . Porcine pancreas lipase (PPL, 46.0 U/g solid), and Candida rugosa lipase (CRL, 1.4 U/g) were obtained from Sigma-Aldrich ® . (iii) Esterase, immobilized in Eupergit ® C from hog liver (~200 U/g) was obtained from Sigma-Aldrich ® .
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