Penicillin acylase (PA) |
Modified macroporous adsorption resin (MAR) |
Temperature of 35 º C, time of 10 h |
6,0 |
Enzymatic stabilization |
There was maintenance of the catalytic activity (2500 U g-1) of PA after 50 cycles |
142142 Akladious, A.; Azzam, S.; Hu, Y.; Feng, P.; CNS Neurosci. Ther.
2018, 6, 549.
|
Protein ficin extract |
Glioxil-agarose |
10 g of glyoxyl agarose in 100 ml of ficin extract solution (1 mg ml-1) prepared in 50 mM sodium carbonate at pH 10.0 at room temperature under continuous stirring |
10 |
Enzymatic stabilization under drastic conditions |
It allowed the stabilization of the enzyme about 40 times |
143143 Ma, X.; Fang, C.; Yan, J.; Zhao, Q.; Tu, Y.; Talanta
2018, 186, 206.
|
Lipase from Burkholderia cepacia (BCL) |
Egg Shell Membrane (ESM) and Oxidized Egg Shell Membrane (ESM) |
Temperature of 30 º C, incubation from 0.5 to 8 h |
7,0 |
Enzymatic stabilization |
Catalytic efficiency in hydrolysis (100%) and transesterification (85%) after 10 cycles |
144144 Pinto, T. V.; Sousa, C. M.; Sousa, C. A. D.; Aboelhassan, M. M.; Peixoto, A. F.; Pereira, C.; Coelho, P. J.; Freire, C.; Dalton Trans.
2017, 46, 9076.
|
Y. lipolytica lipase |
Macroporous adsorbent resin DA201-C |
0.01 g lipase / g resin, 25 º C and adsorption for 3 h |
- |
Catalyze the synthesis of geranyl propionate |
The maximum esterification rate of 87.5%, resulting in an increase of 28.5% over the free enzyme |
145145 Piazzoli, A.; Antonelli, M.; Water Air Soil Pollut.
2018, 229, 193.
|
Lipase de Thermomyces lanuginosus (TLL) |
Mesoporous poly (styrene-divinylbenzene) (PSty-DVB) resin |
150 mg g-1 carrier, 900 min incubation in 5 mM sodium acetate and 25 ºC |
5,0 |
Improving the catalytic activity of Lipase from Thermomyces lanuginosus (TLL) |
Hydrolytic activity of 443.0 ± 25.2 IU g-1 support. High esterification activity and stability in the synthesis of cetyl linoleate (conversion of 90.5 ± 0.6% after five reaction cycles of 30 min each) |
146146 Li, C.; Kumar, S.; Biomass Convers. Biorefinery
2016, 6, 407.
|
Lipases from Candida antarctica (form A(CALA) and form B (CALB)), Thermomyces lanuginosus (TLL), Rhi-zomucor miehie (RML) and phospholipase Lecitase Ultra
|
Spheres of octyl agarose |
10 g of octylagarose in enzymatic solution (0.2 mg protein / ml) in 5 mM sodium phosphate and 25 ºC and continuous stirring at 200 rpm |
7,0 |
Purification of lipases |
Candida antarctica lipase B (CALB) showed better stability in low load concentration biocatalysts. The enzymes were inactive at pH 5, 7 or 9, but active in organic solvents. The use of ethanol promoted stabilization in highly charged biocatalysts, presenting properties similar to the biocatalysts with reduced load |
147147 Nezampour, F.; Ghiaci, M.; Masoomi, K.; J. Chem. Eng.
2018, 63, 1977.
|
Lipase B from Candida antarctica (CALB) and Rhizomucor miehei lipase (RML) |
Modified chitosan with alkyl chains of different sizes |
40 mL of enzyme solution with 1 g of support at 25 º C for 24 h. The enzymatic solution (0.38, 0.50, 0.75 mg protein mL-1) was pre-prepared in 25 mM phosphate buffer |
7,0 |
Supporting production for immobilization of enzymes used in hydrolysis reactions |
CALB immobilized on dodecyl chitosan improved its thermal stability and high selectivity in the hydrolysis of PUFA in DHA and the hydrolysis result was maintained after 5 cycles. For the RML enzyme butyl chitosan presented better results for the hydrolysis reactions, but with low reproducibility in reaction cycles |
148148 Borlido, L.; Moura, L.; Azevedo, A. M.; Roque, A. C. A.; Aires-Barros, M. R.; Farinha, J. P.; S. Biotechnol. J.
2013, 8, 709.
|
Rhus laccase vernicifera
|
Sepiolite, sepiolite modified with chitosan, sepiolite plus Cu (II) and sepiolite modified with chitosan and Cu (II) |
12 mg of dried laccase powder in 8 ml of phosphate buffer solution (10 mM) and filtered with a 0.45 µm membrane. Aliquots of this solution were mixed the adsorbent dispersion. The mixture wa stirred in the dark at 25 º C for 24 h |
7,0 |
Improve catalytic activity |
The adsorbed laccase in sepiolite, sepiolite-Cu-chitosan and sepiolite-chitosan increased their activity, respectively, in 250, 700 and 500% in relation to the non-adsorbed enzyme. The adsorbed laccase desorption was less than 10% and the non-desorbed enzyme maintained high activity at 20 cycles |
149149 Jiang, H.; Sun, M.; Xu, J.; Lu, A.; Shi, Y.; CLEAN -- Soil, Air, Water
2016, 44, 1146.
|
Lipase from Thermomyces lanuginosus (TLL) |
Octyl agarose (OC) |
1, 6 or 30 mg protein g-1 wet support. 5 mM sodium phosphate solution at pH 7.0. The suspension was filtered and the solid washed 10 times with 10 volumes of distilled water and stored at 4 ºC. Wash 100 times with 3M NaCl or 60% glycine, after washing with distilled water |
7,0 |
Enzymatic stabilization |
At pH 7.0, the preparation using 6 mg of lipase is somewhat more stable. At pH 5.0 the biocatalyst with 30 mg was the most stable and at pH 9.0 all the biocatalysts showed similar behavior. In 3 M NaCl the residual activity of the overloaded preparation (30 mg) was 80%. The stability of immobilized TLL is improved by using glycerin |
150150 Khoobi, M.; Motevalizadeh, S. F.; Asadgol, Z.; Forootanfar, H.; Shafiee, A.; Faramarzi, M. A.; Mater. Chem. Phys.
2015, 149, 77.
|
Trypsin, bromelain, and proteolytic complex from hepatopancreas of crab |
Chitosan or enzyme solution on a modified celulose carrier (DAC), chitosan gel |
The cellulose chargers were placed in enzymatic solution or chitosan gel for 2 hours at room temperature. The materials were dried at room temperature for 20 hours; 1 to 2 mg of immobilized protein g-1 of carriers was obtained and the amount of chitosan was 30 mg g-1 of carrier |
8,0 |
To evaluate the enzymatic activity of the immobilized proteins |
Chitosan stabilized the proteins analyzed during drying and storage: for the proteolytic complex of crab hepatopancreas (PC) above 150%, and for bromelain - 600%. Moisture content equal to or greater than 5% caused the inactivation of the enzymes studied |
151151 Chen, B.; Zhao, X.; Liu, Y.; Xu, B.; Pan, X.; RSC Adv.
2015, 5, 1398.
|
Candida antarctica lipases (A (CALA) and B (CALB)), Thermomyces lanuginosus (TLL), Rhizomucor miehei (RML) and Candida rugosa (CRL) and a phospholipase (Lecitase ultra, LU) |
Octyl-glutamic heterocunctional agarose (OCGLU) and octyl-agarose (OC) |
1 or 10 mg of protein per g of support (OC). 50 mM sodium phosphate at pH 7. Add 20 g of carrier in 200 ml of enzyme solution at 25 º C under gentle agitation. The material was filtered and washed several times with distilled water and stored at 4 º C. For OCGLU, the immobilized enzyme was filtered, washed and resuspended in 5 mM sodium acetate buffer at pH 4 and 25 º C for a minimum period of 12 h |
7,0 |
Enzymatic stabilization |
OCGLU has shown to be more advantageous in relation to OC support due to its better adsorption of the enzymes in organic media or non-cationic detergents |
152152 Muhammad, G.; Hussain, M. A.; Amin, M.; Hussain, S. Z.; Hussain, I.; Abbas Bukhari, S. N.; Naeem-ul-Hassan, M.; RSC Adv.
2017, 7, 42900.
|