Polyacrylamide Gel-Entrapped Maltase: An Excellent Design of Using Maltase in Continuous Industrial Processes

Nawaz, Muhammad Asif; Aman, Afsheen; Rehman, Haneef Ur; Bibi, Zainab; Ansari, Asma; Islam, Ziaul; Khan, Iltaf; Qader, Shah Ali Ul

doi:10.1007/s12010-016-2001-3

Cited by 7 publications

(3 citation statements)

References 49 publications

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“…This finding suggests that starch being the substrate of high molecular weight, faced resistance while entering into the microenvironment of gel blocks and interacting with the binding sites of enzymes resulting in the increased requirement of substrate for optimal enzyme activity. Similar finding was reported previously for maltase entrapped in polyacrylamide gel (Nawaz et al 2016). Vmax of entrapped enzyme in polyacrylamide was also found to decrease by 1.877 fold.…”

Section: Discussionsupporting

confidence: 91%

Fabrication of 1,4-alpha-D-glucan glucanohydrolase holding Gel-Scaffolds using Agar-Agar, a natural polysaccharide and Polyacrylamide, a synthetic organic polymer for continuous liquefaction of starch

et al. 2023

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1,4-alpha-D-glucan glucanohydrolase is among the most widely used commercial hydrolytic enzymes acting randomly on the glycosidic linkages of starch resulting in its saccharification and liquefaction. Its applicability in different industries can be improved by enhancing its stability and reusability. Therefore, in the present study attempts have been made to enhance the industrial applicability of 1,4-alpha-D-glucan glucanohydrolase from Bacillus subtilis KIBGE-HAR by adapting immobilization technology. The study developed mechanically stable, enzyme containing gel-frameworks using two support matrices including agar-agar, a natural polysaccharide and polyacrylamide gel, a synthetic organic polymer. These catalytic gel-scaffolds were compared with each other in terms of kinetics and stability of entrapped 1,4-α-D-glucan glucanohydrolase. In case of polyacrylamide gel, Km value for immobilized enzyme increased to 7.95 mg/mL, while immobilization in agar-agar resulted in decreased Km value i.e 0.277 mg/mL as compared to free enzyme. It was found that immobilized enzyme showed maximum activity at 70 °C in both the supports as compared to free enzyme having maximum activity at 60 °C. Immobilized 1,4-α-D-glucan glucanohydrolase exhibited no change in optimal pH 7.0 before and after entrapment in polyacrylamide gel and agar-agar. The enzyme containing gel-scaffold was found suitable for repeated batches of starch liquefaction in industrial processes. Agar-agar entrapped 1,4-α-D-glucanglucanohydrolase was capable to degrade starch up to seven repeated operational cycles whereas polyacrylamide entrapped enzyme conserved its activity up to sixth operational cycle.

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Section: Discussionsupporting

confidence: 91%

Fabrication of 1,4-alpha-D-glucan glucanohydrolase holding Gel-Scaffolds using Agar-Agar, a natural polysaccharide and Polyacrylamide, a synthetic organic polymer for continuous liquefaction of starch

et al. 2023

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“…Poly (acrylamide) (PAM) is a commonly used synthetic polymer with a range of applications in materials processing 14 and biotechnology [51][52] . It forms strong IPCs with a range of materials, including poly(acrylic acid) (PAA).…”

Section: Introductionmentioning

confidence: 99%

Förster Resonance Energy Transfer across interpolymer complexes of poly(acrylic acid) and poly(acrylamide)

Swift

Paul

Swanson

et al. 2017

Polymer

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Interpolymer complexes of homopolymer macromolecules are often described as 'laddered' or 'ribbon' type structures. The proposition of the existence of these ladder structures seems to us not reasonable and here we examine this hypothesis. To address this we have used polymers enabled for Förster Energy Transfer (FRET). Chromophores bound to a macromolecular backbone can transfer energy across short distances via FRET. The close binding of poly(acrylamide) and poly(acrylic acid) interpolymer complex formation at low pH forms a structure compact enough for significant energy transfer to occur between different chains containing naphthalene and anthracene labels. In the context of the proposition that ladder polymers can form it was surprising that the distance between labels on the same polymer backbone was equivalent regardless of whether the polymer was complexed or not. The data indicated that the bicomponent structure may be more compact than previously supposed: I.e. the complexes are not ladders composed of extended chains. This evidence suggests formation not of ordered 'ladder' systems but colloidal 'co-globules'.

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“…The reactivity and stability of encapsulated enzymes are depended on porous structure of gel and higher pore size of gel may outflow the enzymes from the gel, and lower size may restrict the entery of substrate into the gel. The concentration acrylamide and crosslinker define the pore size of gel, so the optimiztaion of concentration ratio of acrylamide and crosslinker is necessary to trap the enzyme within gel and make the substrate and product exchangeable across the porous structure of gel [ 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

Encapsulation of pectinase within polyacrylamide gel: characterization of its catalytic properties for continuous industrial uses

Rehman

Nawaz

Pervez

et al. 2020

Heliyon

Self Cite

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Pectinase as a biocatalyst play a significant role in food and textile industries. In this study, the pectinase was immobilized by encapsulation within polyacrylamide gel to enhance its catalytic properties and ensure the reusability for continuous industrial processes. 9.5% acrylamide and 0.5% N, N′- methylenebisacrylamide concentration gave high percentage of pectinase immobilization yield within gel. The catalytic properties of immobilized pectinase was determined with comparison of soluble pectinase. The immobilization of pectinase within polyacrylamide gel didn't effect catalytic properties of pectinase and both the free and immobilized pectinase showed maximum pectinolytic activity at 45 °C and pH 10. The Michaelis-Menten kinetic behavior of pectinase was slightly changed after immobilization and immobilized pectinase showed somewhat higher K m and lower V max value as compared to soluble pectinase. Polyacrylamide gel encapsulation enhanced the thermal stability of pectinase and encapsulated pectinase showed higher thermal stability against various temperature ranging from ranging from 30 °C to 50 °C as compared free pectinase. Furthermore, the surface topography of polyacrylamide gel was analyzed using scanning electron microscopy and it was observed that the surface topography of polyacrylamide gel was changed after encapsulation. The encapsulation of pectinase within polyacrylamide gel enhanced the possibility of reutilization of pectinase in various industries and pectinase retained more than 50% of its initial activity even after seven batch of reactions.

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Polyacrylamide Gel-Entrapped Maltase: An Excellent Design of Using Maltase in Continuous Industrial Processes

Cited by 7 publications

References 49 publications

Fabrication of 1,4-alpha-D-glucan glucanohydrolase holding Gel-Scaffolds using Agar-Agar, a natural polysaccharide and Polyacrylamide, a synthetic organic polymer for continuous liquefaction of starch

Fabrication of 1,4-alpha-D-glucan glucanohydrolase holding Gel-Scaffolds using Agar-Agar, a natural polysaccharide and Polyacrylamide, a synthetic organic polymer for continuous liquefaction of starch

Förster Resonance Energy Transfer across interpolymer complexes of poly(acrylic acid) and poly(acrylamide)

Encapsulation of pectinase within polyacrylamide gel: characterization of its catalytic properties for continuous industrial uses

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