Immobilization of alpha-amylase (Termamyl® 2X) in Duolite® A-568 resin

Silva, Fernanda dos Santos; Pio, Flávia Souza; Ribeiro, Eloízio Júlio; Resende, Miriam Maria de

doi:10.1016/j.bcab.2023.102661

Cited by 4 publications

(3 citation statements)

References 27 publications

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“…The broad space for the Alpha-amylase immobilization method caused researchers to combine the two methods. Immobilization of Thermamyl 2X Alpha-amylase with a combined method of adsorption and crosslinking on duolite A-568 resin exchange matrix [31]. The optimum immobilized Alpha-amylase was obtained at pH 7, used 3 times, and could be stored for 25 days.…”

Section: Immobilized Alpha-amylasementioning

confidence: 99%

The use of immobilized enzyme in starch bioconversion: An update review

Miftahuddin,

Laga,

Bastian

2024

BIO Web Conf.

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Starch bioconversion enzymes play an important role in the food industry, raising up a vast research space. Immobilization of alpha-amylase, amyloglucosidase and glucose isomerase is a promising topic for ongoing research. In this review, we provide an updated overview of various carriers for carbohydrases immobilization, with the primary focus on the food industry. The method used in this review is the literature study method. The immobilization methods of carbohydrases enzymes are encapsulation by Ca-alginate, covalent and ionic bonding by chitosan, adsorption by ion exchange resin and cross-linking by glutaraldehyde and Bovine serum albumin as protein feeder, and mix of them. The research shows the ability of enzymes that can be used repeatedly while maintaining their activity. Immobilization increases the enzymes stability towards pH, temperature, and type of substrate. Through this method, various types of sugar such as maltose, glucose and fructose can be produced with reduced production costs. In future, immobilized enzymes are going to play a vital role in various industries not only in food, but including pharmaceuticals, chemicals, and fuel.

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Section: Immobilized Alpha-amylasementioning

confidence: 99%

The use of immobilized enzyme in starch bioconversion: An update review

Miftahuddin,

Laga,

Bastian

2024

BIO Web Conf.

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“…The maximum activity was observed at immobilization pH 7, contact period of support and enzyme at 60 minutes, initial amount of protein of 1mg and immobilization temperature of 40 • C were taken as the optimum immobilization parameter. (19,25,26) .…”

Section: Optimization Of Immobilisation Of Free Enzymesmentioning

confidence: 99%

Aniline Formaldehyde Cross-Linked Polyaniline Magnetic Nanocomposite with Core-Shell Structure As A New Platform for Enzyme Immobilization

Augustine¹,

Geetha²,

Dhanya³

et al. 2023

IJST

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Objectives:The industrial application of an enzyme is governed by its thermodynamic properties and stability, which can be effectively improved by immobilizing enzymes onto suitable supports. The present work is done by immobilizing α-amylase onto aniline formaldehyde condensate cross-linked polyaniline magnetic nanocomposite. Methods: Physiochemical characterization of synthesized Fe 3 O 4 -CLPANI nanocomposite was done by FT-IR, XRD, TG, and SEM images. Biochemical characterization related to immobilization efficiency, the kinetic parameters Vmax and the Km value, thermal stability, storage stability and reusability of immobilized enzymes were determined. Findings: Both physiochemical and biochemical characterization led to the conclusion that Fe 3 O 4 -CLPANI immobilized amylase indicated better thermal stability than that of free enzyme and it tailored to the requirement as an industrial catalyst. Novelty: To the best of our knowledge, no literature is available on the immobilization of the enzyme to Fe 3 O 4 -CLPANI composites with core-shell structure.

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“…When selecting the support for enzyme immobilization, it is crucial to consider the characteristics of the enzyme and choose the appropriate functional groups and immobilization conditions. Supports like agarose beads [ 32 ], zeolites [ 33 ], porous glass [ 34 ], and epoxy resins [ 35 ] offer a large surface area for enzyme-support interactions. However, it is important to note that glutaraldehyde chemistry, while being a popular technique, determines the chemical modification of the entire enzyme surface [ 36 , 37 ].…”

Section: Introductionmentioning

confidence: 99%

An Accessible Method to Improve the Stability and Reusability of Porcine Pancreatic α-Amylase via Immobilization in Gellan-Based Hydrogel Particles Obtained by Ionic Cross-Linking with Mg2+ Ions

et al. 2023

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Amylase is an enzyme used to hydrolyze starch in order to obtain different products that are mainly used in the food industry. The results reported in this article refer to the immobilization of α-amylase in gellan hydrogel particles ionically cross-linked with Mg2+ ions. The obtained hydrogel particles were characterized physicochemically and morphologically. Their enzymatic activity was tested using starch as a substrate in several hydrolytic cycles. The results showed that the properties of the particles are influenced by the degree of cross-linking and the amount of immobilized α-amylase enzyme. The temperature and pH at which the immobilized enzyme activity is maximum were T = 60 °C and pH = 5.6. The enzymatic activity and affinity of the enzyme to the substrate depend on the particle type, and this decreases for particles with a higher cross-linking degree owing to the slow diffusion of the enzyme molecules inside the polymer’s network. By immobilization, α-amylase is protected from environmental factors, and the obtained particles can be quickly recovered from the hydrolysis medium, thus being able to be reused in repeated hydrolytic cycles (at least 11 cycles) without a substantial decrease in enzymatic activity. Moreover, α-amylase immobilized in gellan particles can be reactivated via treatment with a more acidic medium.

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Immobilization of alpha-amylase (Termamyl® 2X) in Duolite® A-568 resin

Cited by 4 publications

References 27 publications

The use of immobilized enzyme in starch bioconversion: An update review

The use of immobilized enzyme in starch bioconversion: An update review

Aniline Formaldehyde Cross-Linked Polyaniline Magnetic Nanocomposite with Core-Shell Structure As A New Platform for Enzyme Immobilization

An Accessible Method to Improve the Stability and Reusability of Porcine Pancreatic α-Amylase via Immobilization in Gellan-Based Hydrogel Particles Obtained by Ionic Cross-Linking with Mg2+ Ions

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