Polyvinyl alcohol–silica nanohybrids: An efficient carrier matrix for amylase immobilization

Singh, Vandana; Singh, Devendra Kumar

doi:10.1016/j.procbio.2012.10.017

Cited by 31 publications

(10 citation statements)

References 30 publications

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“…It was observed that the immobilized enzyme demonstrated 75% activity after 10 runs. It was found that, the reuse capability of α-amylases was in the 50%–88% activity range after 5–25 runs [17,18,25,26,27].…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

et al. 2014

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α-Amylase from Trichoderma harzianum was covalently immobilized on activated wool by cyanuric chloride. Immobilized α-amylase exhibited 75% of its initial activity after 10 runs. The soluble and immobilized α-amylases exhibited maximum activity at pH values 6.0 and 6.5, respectively. The immobilized enzyme was more thermally stable than the soluble one. Various substrates were hydrolyzed by immobilized α-amylase with high efficiencies compared to those of soluble α-amylase. The inhibition of the immobilized α-amylase by metal ions was low as compared with soluble enzyme. On the basis of the results obtained, immobilized α-amylase could be employed in the saccharification of starch processing.

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Section: Resultsmentioning

confidence: 99%

Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

et al. 2014

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“…In order to study the kinetic effect of the immobilization, the rates of the starch hydrolysis by the free α ‐amylase and immobilized α ‐amylase were measured at various starch concentrations. The relation between substrate concentration and rate of enzymatic reaction can be described by Michaelis–Menten equation, which can be represented into linear form as Lineweaver–Burk equation for computation of V max and K m values . The Lineweaver–Burk plots of the free and immobilized α ‐amylases were given in Fig.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of α‐amylase on reactive modified fiber and its application for continuous starch hydrolysis in a packed bed bioreactor

Temoçin

2013

Starch Stärke

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In this study, the enzyme α‐amylase was immobilized on reactive modified poly (ethylene terephthalate) fiber. The activities of free α‐amylase and immobilized α‐amylase were compared in a batch starch hydrolysis system. Optimum pH and Michaelis–Menten constants were determined for both free α‐amylase and immobilized α‐amylase. The immobilization shifted the optimum pH to a higher level. The Michaelis–Menten constant values (Km) of the immobilized α‐amylase and free α‐amylase were obtained as 11.94 and 6.61 mg/mL, respectively. The experiments indicated that the immobilization increased the thermal stability of the α‐amylase. The immobilized α‐amylase, easily separated from the reaction media, could be used effectively for 15 cycles with 65% retention of the initial activity. Moreover, the immobilized α‐amylase was effectively used in packed bed bioreactor for continuous starch hydrolysis throughout 6.5 h without loss of activity. Different starches (e.g., potato and wheat) were hydrolyzed by the immobilized α‐amylase in continuous process. The results indicate a potential use of this immobilized enzyme system for the construction of packed bed bioreactors to be used in the hydrolysis of the starch.

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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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Polyvinyl alcohol–silica nanohybrids: An efficient carrier matrix for amylase immobilization

Cited by 31 publications

References 30 publications

Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

Immobilization of α‐amylase on reactive modified fiber and its application for continuous starch hydrolysis in a packed bed bioreactor

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

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