Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase of<i>Aspergillus nidulans</i>

Peña-Montes, Carolina; Mondragón-Tintor, María Elena; Castro-Rodríguez, José Augusto; Bustos‐Jaimes, Ismael; Navarro‐Ocaña, Arturo; Farrés, Amelia

doi:10.1155/2013/928913

Cited by 14 publications

(8 citation statements)

References 47 publications

(58 reference statements)

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“…Percent C of the drug also found to be high in immobilized-lipase AP6 catalysed study. The results obtained were in line with Peña-Montes et al [42] . According to them, the recombinant NStcI esterase of A. nidulans has retained its pharmacological activity and enantioselectivity after immobilization for longer periods, when compared to that of the free-enzyme.…”

Section: Incubated With Whole-cell and Immobilized-cell Culturessupporting

confidence: 92%

Enantioselective Conversion of Racemic Sotalol to R(-)-Sotalol by Lipase AP6

Swetha¹,

Vijitha²,

Veeresham³

2018

pharmaceutical-sciences

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Most pharmaceutical compounds have asymmetric nature and are optically active. Compounds with one asymmetric centre (chiral centre) would exhibit two enantiomeric forms and among them one is pharmacologically active (eutomer) while the other one contributed side effects or toxic effects or totally inert (distomer) [1] . Hence, current interest is towards development and administration of eutomer instead of its racemic mixture to improve therapeutic efficacy and reduce the unwanted effects due to the distomer [2] . Biocatalysts have excellent selectivity under mild reaction conditions [2] and hence in this study various whole-cell microorganisms like Bacillus subtilis [3] , Escherichia coli [4] , Pseudomonas putida [5] , Sphingomonas paucimobilis [6] , Rhodococcus erythropolis [7] , Streptomyces halstedii [8] , Aspergillus niger [9] , Candida parapsilosis [10] , Geotrichum candida [11] , Rhizopus oryzae [12] , Cunninghamella elegans [13] and Cunninghamella blakesleeana [14] were employed as biocatalysts for the stereo inversion of racemic sotalol to its active enantiomer. However, a limitation for using whole-cell microorganisms as biocatalysts is reduced stereo selectivity due to competition between multiple enzymes of the microorganism for the same substrate [15] . The use of isolated pure enzymes with suitable cofactors as biocatalysts would help overcome this limitation of using whole-cell microorganisms [16] and the reactions catalysed by pure enzymes also serves some other advantages like they are highly selective under mild conditions, more catalytic in nature and environmentally benign [2] . Lipases have great versatility in catalysing different reactions like aminolysis, esterification, transesterification and interesterification. The means followed by lipases to catalyse these reactions can be described as a ping-pong bi-bi mechanism. Accordingly, first step involves nucleophilic attack on the carbonyl group of a drug, which results in acyl-

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Section: Incubated With Whole-cell and Immobilized-cell Culturessupporting

confidence: 92%

Enantioselective Conversion of Racemic Sotalol to R(-)-Sotalol by Lipase AP6

Swetha¹,

Vijitha²,

Veeresham³

2018

pharmaceutical-sciences

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“…This is because the carboxyl groups of alginate and amino and carboxyl groups of chitosan along with their good hydrophilicity and high porosity create a link with enzymes [ 22 ]. According to Peña-Montes et al [ 23 ] the ionic interactions between the enzyme and the support improves the conformational stability of the immobilized enzyme, thereby providing longer shelf life. However, at chitosan concentrations above 0.3% the gelling solution was very viscous for application, causing agglomeration or aggregation of the surface of the microcapsules during formation.…”

Section: Resultsmentioning

confidence: 99%

High Catalytic Activity of Lipase from Yarrowia lipolytica Immobilized by Microencapsulation

Pereira

Fraga

Diniz

et al. 2018

IJMS

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Microencapsulation of lipase from Yarrowia lipolytica IMUFRJ 50682 was performed by ionotropic gelation with sodium alginate. Sodium alginate, calcium chloride and chitosan concentrations as well as complexation time were evaluated through experimental designs to increase immobilization yield (IY) and immobilized lipase activity (ImLipA) using p-nitrophenyl laurate as substrate. To adjust both parameters (IY and ImLipA), the desirability function showed that microcapsule formation with 3.1%(w/v) sodium alginate, 0.19%(w/v) chitosan, 0.14 M calcium chloride, and 1 min complexation time are ideal for maximal immobilization yield and immobilized lipase activity. A nearly twofold enhancement in Immobilization yield and an increase up to 280 U/g of the lipase activity of the microcapsules were achieved using the experimental design optimization tool. Chitosan was vital for the high activity of this new biocatalyst, which could be reused a second time with about 50% of initial activity and for four more times with about 20% of activity.

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“…The flow through was collected to calculate the loading efficiency of the immobilized beads. The loading efficiency and the immobilization yield of the beads were computed by the method described by Peña-Montes (2013). The prepared beads were stored in 10 mM Tris-HCl buffer at 4 °C.…”

Section: Immobilization Of Isolated Esterasementioning

confidence: 99%

Enhancing the stability of a carboxylesterase by entrapment in chitosan coated alginate beads

Raghu¹,

Pennathur²

2018

Turk J Biol

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Introduction Esterases are hydrolytic enzymes that cleave ester bonds, liberating alcohol and carboxylic acid (E.C 3.1.1.1). They have a wide range of applications in food processing, beverages, and perfume industries (Panda and Gowrishankar, 2005). Microorganisms produce different types of esterases, and are unique in catalyzing specific reactions. For example, arylesterase obtained from Saccharomyces cerevisiae is used for enhancing flavor in alcoholic beverages (Lomolino et al., 2003). Similarly sterol esterases isolated from Pseudomonas sp., Chromobacterium, and Ophiostoma picea are used by the paper industry to reduce problems of pitch during paper making (Kontkanen et al., 2004). The genus Aeromonas is ubiquitous in the environment; they are found in fresh water, drinking water, and saline water. Cold-adapted lipases have been isolated from Aeromonas LPB4 from deep sea sediments and A. hydrophila from food products (Soltan et al., 2016). Immobilized enzymes are preferred over free enzyme because they can be used for many reaction cycles and can be separated easily from the final product. Immobilization leads to conformational changes in the enzyme thus altering many of its properties and can lead to enhanced activity and stability (Mateo et al., 2007). Enzyme immobilization by entrapment is a technique by which the free enzyme is secured in a semipermeable support material, and this prevents the enzyme from diffusing while allowing substrates and products to pass through freely (Won et al., 2005). These support materials can be natural polymers such as cellulose, agar, chitin, alginate, dextrans, or synthetic polymers, such as polystyrene, polyacrylate, polymethacrylate, vinyl, and allyl polymers. Recently, a silica based solid binding peptide was used as a support material for the immobilization of hemicellulase enzyme. The immobilized enzyme was used for the catalysis of simple and complex polysaccharides (Care et al., 2017). Amongst all the polymers mentioned, alginate is the most commonly used due to its thermostability and nontoxicity. A type of esterase (lipase B) obtained from Candida antarctica was immobilized on chitosan-alginate complex, which was functionalized by a few covalent modifications. The immobilized enzyme was used for the synthesis of butyl oleate (Silva et al., 2011). Alginates are commercially available as sodium alginate. Alginate is a

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Immobilization and Biochemical Properties of the Enantioselective Recombinant NStcI Esterase ofAspergillus nidulans

Cited by 14 publications

References 47 publications

Enantioselective Conversion of Racemic Sotalol to R(-)-Sotalol by Lipase AP6

Enantioselective Conversion of Racemic Sotalol to R(-)-Sotalol by Lipase AP6

High Catalytic Activity of Lipase from Yarrowia lipolytica Immobilized by Microencapsulation

Enhancing the stability of a carboxylesterase by entrapment in chitosan coated alginate beads

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