Immobilization of β-amylase on polystyrene cation exchange resin equilibrated with Al3+ions (IR-120 Al3+)

Roy, F. P. Van; Hegde, Mahabaleshwar V.

doi:10.1016/0141-0229(87)90086-x

Cited by 10 publications

(6 citation statements)

References 16 publications

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“…Both preparations have better results when citratephosphate buffer was used, but the free enzyme presented optimal pH value at pH 6.0, while the immobilized amylase had a maximum activity at pH 6.5. Roy and Edge [33] also observed an increase in the optimum pH, from 5.0 to 5.6. Very interestingly, the immobilized amylase maintained high activity in all the range of pH values studied, even in the most extreme ones (pH 3.0, and 10.0), while the free enzyme dramatically decreased its activity by just moving one pH unit far from the optimal pH value.…”

Section: Characterization Of the Beta Amylase Immobilized On Glutaralmentioning

confidence: 77%

“…The Km for the free enzyme was very near to our study (2.4 mg mL −1 ). In Roy and Edge's [33] study, when the enzyme was immobilized on polystyrene cation exchange resin equilibrated with Al 3+ íons, its Km increased about 6 times. Differences on the particles size, pores diameter and enzyme loading may drastically influence the effect of diffusional limitations on the expressed activity of immobilized enzymes [15,22].…”

Section: Kinetic Parameters Of Beta-amylase Immobilized On Glutaraldementioning

confidence: 98%

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Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

Tavano

Fernández-Lafuente

Goulart

et al. 2013

Process Biochemistry

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A simplified procedure for the preparation of immobilized beta-amylase using non-purified extract from fresh sweet potato tubers is established in this paper, using differently activated agarose supports. Beta-amylase glutaraldehyde derivative was the preparation with best features, presenting improved temperature and pH stability and activity. The possibility of reusing the amylase was also shown, when this immobilized enzyme was fully active for five cycles of use. However, immobilization decreased enzyme activity to around 15%. This seems to be mainly due to diffusion limitations of the starch inside the pores of the biocatalyst particles. A fifteen-fold increase in the Km was noticed, while the decrease of Vmax was only 30% (10.1 U mg −1 protein and 7.03 U mg −1 protein for free and immobilized preparations, respectively).

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Section: Characterization Of the Beta Amylase Immobilized On Glutaralmentioning

confidence: 77%

Section: Kinetic Parameters Of Beta-amylase Immobilized On Glutaraldementioning

confidence: 98%

Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

Tavano

Fernández-Lafuente

Goulart

et al. 2013

Process Biochemistry

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“…The enzyme exhibited optimal activation at a more alkaline pH (5.6 compared to 5.0) and a broader temperature range (45−55 °C, compared to 45 °C), than the unsupported enzyme. The K m of the enzyme increased 6-fold upon immobilization, and it retained ∼60% of its initial activity after 120 days of storage at room temperature …”

Section: Ion-exchange Resin-supported Enzymesmentioning

confidence: 99%

Organic Synthesis by Catalysis with Ion-Exchange Resins

Gelbard

2005

Ind. Eng. Chem. Res.

180

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This review is intended to give a wide scope on the uses of ion-exchange resins as catalysts or catalyst precursors in organic synthesis, for the preparation of fine or intermediate chemicals. Twelve families of reaction have been covered and presented according to the molecules to be synthesized, regardless of the anionic or cationic nature of the resins; thus, ∼300 references have been selected from January 1980. In acid-catalyzed reactions, the contribution of both Lewis acidity and Bro ¨nsted acidity are mentioned, and, when available, some aspects related to the stability or the recycling of the catalysts are reported. In base-catalyzed reactions, the importance of the thermal stability of anionic resins has been underlined. A table that is included as an appendix provides some data on the resins quoted here.

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“…Natural cellulose satisfies most of these requirements, and is readily available in Roy & Hegde, 1987Nakanishi et al, 1983Sharma & Yamazaki, 1984Dominquez et al, 1988Kierstan et al, 1982Lee & Woodward, 1983Hahn-Hagerdal, 1984Sharma & Yamazaki, 1984AXfzmetal, 1987Fujikawa et al, 1988Roy etai, 1989Roy etal, 1989Husain & Saleemuddin, 1989Oguntimein & Reilly, 1980Woodward & Zachry, 1982Tomar & Prabhu, 1985Strandberg & Smiley, 1972Chen et al, 1981Imai etal., 1986Nakakxte et al, 1983 4 a variety of different forms (fibres, powders and papers). Reactive sites in cellulose may be generated for the covalent attachment of proteins (Chen et al, 1981;Cannon et al, 1984;Tomar & Prabhu, 1985;Jin & Toda, 1988;Dumitriu et al, 1989).…”

Section: List Of Tablesmentioning

confidence: 99%

Enzyme Immobilization Using the Cellulose-Binding Domain of a Cellulomonas Fimi Exoglucanase

et al. 1989

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In presenting this thesis in partial fulfilment of the requirements for an advanced degree at the University of British Columbia, I agree that the Library shall make it freely available for reference and study. I further agree that permission for extensive copying of this thesis for scholarly purposes may be granted by the head of my department or by his or her representatives. It is understood that copying or publication of this thesis for financial gain shall not be allowed without my written permission.

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Immobilization of β-amylase on polystyrene cation exchange resin equilibrated with Al3+ions (IR-120 Al3+)

Cited by 10 publications

References 16 publications

Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

Optimization of the immobilization of sweet potato amylase using glutaraldehyde-agarose support. Characterization of the immobilized enzyme

Organic Synthesis by Catalysis with Ion-Exchange Resins

Enzyme Immobilization Using the Cellulose-Binding Domain of a Cellulomonas Fimi Exoglucanase

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