Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline

Radovanović, Mirjana; Jugović, Branimir; Gvozdenović, Milica M.; Jokić, Bojan; Grgur, Branimir N.; Bugarski, Branko; Knežević‐Jugović, Zorica

doi:10.1002/star.201500161

Cited by 17 publications

(11 citation statements)

References 33 publications

(42 reference statements)

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“…In this context, design of a suitable amylase immobilization process and optimization of its operating conditions are very important for industrial applications [7]. a-Amylase has been immobilized on a wide variety of organic and inorganic supports using different methods [13][14][15][16][17][18][19][20][21]. The methods used can be divided into three categories: binding to a support (carrier), entrapment (encapsulation), and crosslinking.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Cryptococcus flavus α‐amylase on glass tubes and its application in starch hydrolysis

2016

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α‐Amylase from Cryptococcus flavus was previously purified after exchange chromatography on Q‐Sepharose and gel filtration on Sephacryl S‐100. The enzyme was purified 128‐fold with a recovery rate of 81% of activity. The molecular mass of the α‐amylase was 67 kDa as determined by SDS–PAGE. The enzyme was characterized after immobilization on glass tubes. The immobilization yield, efficiency, and activity recovery of α‐amylase were 79, 57, and 45%, respectively. The optimum pH of the immobilized enzyme was shifted to a more acidic pH (4.5) compared with the free enzyme (5.5). The optimum temperature of the immobilized enzyme was the same for the free enzyme (50°C), but it showed a higher thermal stability. The immobilized enzyme showed activity until the 10th cycle, maintaining 47% of initial activity, and was capable of hydrolyzing starch from potato, wheat, corn, and cassava. The main products released from starch were maltose, maltotriose, and maltotetraose.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Cryptococcus flavus α‐amylase on glass tubes and its application in starch hydrolysis

2016

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“…α-Amilaze se primenjuju u prehrambenoj industriji, tekstilnoj, industriji papira, detergenata, itd [21]. Veliki broj istraživača je ispitivao imobilizaciju α-amilaza na modifikovanim i nemodifikovanim magnetnim česticama , ali su veoma retki podaci o primeni polianilina za njihovu stabilizaciju i uticaju na katalitičku aktivnost α-amilaze [25]. Generalno, imobilizacija α-amilaze na polianilinu je nedovoljno proučena i pored nekih očiglednih prednosti koje je dati polimer pokazao pri imobilizaciji tripsina, β-galaktozidaze, glukozo-oksidaze, lipazе i drugih enzima [20,[26][27][28].…”

Section: Izvodunclassified

“…Čestice MAG sintetisane su metodom koprecipitacije Fe 2+ i Fe 3+ u višku amonijaka po postupku opisanom u literaturi [25,26]. Rastvoreno je 5,6 g FeSO 4 ⋅7H 2 O i 10,8 g FeCl 3 ⋅6H 2 O u 300 mL destilovane vode.…”

Section: Sinteza Mag I Mag-paniunclassified

“…S obzirom na to da tokom stvaranja PANI prevlake na MAG ne dolazi do mešanja reakcione smeše ili drugih mehaničkih uticaja koji bi uzrokovali usitnjavanje čestica, pretpostavlja se da je trimodalna raspodela veličine MAG-PANI uzrokovana nastankom samostalnih čestica polanilina koji nisu obložili čestice MAG. Grafik potvrđuje ranije snimljene FESEM mikrografije [25] na osnovu kojih je zaključeno da su MAG i MAG-PANI mikročestice (aglomerati nanočestica).…”

Section: Slika 3raspodela Veličine čEstica Mag (□) I Mag-pani(■) Fiunclassified

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Polyaniline stabilization of magnetic particles and immobilization of α-amylase

Radovanović¹,

Nikolić²,

Djurovic³

et al. 2018

Hem Ind

Self Cite

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Magnetic particles (MAG), obtained by standard procedure of coprecipitation of Fe2+and Fe3+ in an excess of ammonia, and polyaniline modified magnetic particles MAG-PANI were used as carriers for immobilization of ?-amylase from Bacillus licheniformis. The formation of a polyaniline layer (PANI) on MAG particles was achieved by chemical polymerization of aniline. Immobilization was carried out by adsorption, as a simple, inexpensive and fast method that allows retention of a large portion of the initial activity of the immobilized enzyme. FTIR spectroscopy was used to characterize the obtained particles and to confirm changes dueto formation of a PANI layer and conjugation of ?-amylase on the particle surfaces. Particle size distribution was bimodal and three-modal for MAG and MAG-PANI, respectively. Appearance of a fraction of smaller MAG-PANI particles than MAG particles could be attributed to the formation of PANI particles without the MAG core. Measured values of Zeta potential for MAG-PANI were higher as compared to MAG indicating stabilization of particles in the presence of PANI. Relevant kinetic parameters for immobilized enzyme were determined from the Hanes plot. The apparent Km constant was 1.91 and 1.48 g L?1 for MAG-A and MAG-PANI-A, respectively, while ??m was 0.19 g L?1 min?1 for MAG and 0.32 g L?1 min?1 for MAG-PANI. The obtained values of Km indicated that modification of MAG by PANI enhanced kinetic properties of the immobilized enzyme. Moreover, the modification of MAG by PANI showed the increase in both pH and thermal stabilities of the immobilized enzyme. Studies of the operational activity of the immobilized enzyme on MAG-PANI have shown that 98.8% of starch was hydrolyzed over 20.0 min. In the first cycle in the packed bed reactor operated in a recycling mode, but approximately five times longer period was required to hydrolyze 93.5 of starch in the fifth cycle. In the continuous packed bed reactor without recycling, the degree of starch hydrolysis was not changed significantly during 4 h and was 88.8?1.6%, whereas the half-life of the biocatalyst was 6.2 h. Although coating MAG particles with a polyaniline offers many advantages, the main disadvantage is possible appearance of residues of aniline monomers and dimmers. The potential toxicity of these residues requires precise composition analysis of the product of starch hydrolysis catalyzed by ?-amylase adsorbed onto MAG-PANI. [Project of the Serbian Ministry of Education, Science and Technological Development, Grant no. III 46010]

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“…Immobilization also caused an increase in the enzyme stability during storage [64]. Radovanovic and coworkers [65] demonstrated immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline. The obtained magnetic particles were agglomerates of NPs with sizes below 100 nm.…”

Section: α-Amylasementioning

confidence: 99%

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review

Husain¹

2017

Biocatalysis

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Numerous types of nanoparticles and nanocomposites have successfully been employed for the immobilization and stabilization of amylolytic enzymes; α-amylases, β-amylases, glucoamylases and pullulanases. Nano-support immobilized amylolytic enzymes retained very high activity and yield of immobilization. The immobilization of these enzymes, particularly α-amylases and pullulanases, to the nanosupports is helpful in minimizing the problem of steric hindrances during binding of substrate to the active site of the enzyme. The majority of nano-support immobilized amylolytic enzymes exhibited very high resistance to inactivation induced by different kinds of physical and chemical denaturants and these immobilized enzyme preparations maintained very high activity on their repeated and continuous uses. Amylolytic enzymes immobilized on nano-supports have successfully been applied in food, fuel, textile, paper and pulp, detergent, environmental, medical, and analytical fields.

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Immobilization of α-amylase via adsorption on magnetic particles coated with polyaniline

Cited by 17 publications

References 33 publications

Immobilization of Cryptococcus flavus α‐amylase on glass tubes and its application in starch hydrolysis

Immobilization of Cryptococcus flavus α‐amylase on glass tubes and its application in starch hydrolysis

Polyaniline stabilization of magnetic particles and immobilization of α-amylase

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review

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