Immobilised enzymes

Mosbach, Klaus

doi:10.1016/0014-5793(76)80856-3

Cited by 58 publications

(10 citation statements)

References 63 publications

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“…Some form of metabolite compartmentation in erythrocyte glycolysis has been suggested by Niehaus & Hammerstedt (1976), on the basis of the kinetics of incorporation of extracellular P, into ATP in the intact cell, as well as by Friedrich et al (1977), who have used aglycerophosphate dehydrogenase as an 'enzyme probe' to test whether certain metabolites are accessible to the bulk medium in concentrated preparations of sonicated erythrocytes. Some degree of channelling of glycolytic intermediates is suggested by these and the present experiments, and this may be expected to have a profound effect on the flux characteristics of glycolysis in the intact cell (Katchalski et al, 1971;Mosbach, 1976;Wooster & Wrigglesworth, 1976b). The close association of glyceraldehyde 3-phosphate dehydrogenase with phosphoglycerate kinase, another enzyme found to be associated with the membrane fraction after erythrocyte lysis (Tillmann et al, 1975), may also help to control the intracellular concentrations of 2,3-bisphosphoglycerate, a physiological regulator of haemoglobin oxygen affinity (Benesch et al, 1971;Brewer & Eaton, 1971).…”

Section: Discussionsupporting

confidence: 54%

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Keokitichai¹,

Wrigglesworth²

1980

Biochemical Journal

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Intact human erythrocytes were exposed to low concentrations of glutaraldehyde. After washing and subsequent lysis of the cells, glyceraldehyde 3-phosphate dehydrogenase activity is found to be associated with a membrane fraction and cannot be eluted by salt treatment. Lactate dehydrogenase activity is associated with a supernatant fraction under the same conditions. Preincubation of the intact cells under conditions designed to increase internal NADH concentrations, leads to a lower membrane-associated activity of glyceraldehyde 3-phosphate dehydrogenase after lysis.

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Section: Discussionsupporting

confidence: 54%

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Keokitichai¹,

Wrigglesworth²

1980

Biochemical Journal

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“…1,37 Macroporous materials (>50 nm pore diameter) have been employed extensively for enzyme immobilisation. [38][39][40][41] Commercial resins such as Eupergit s and Sepabeads s are popular macroporous supports [42][43][44][45][46] -these traditionally have functional epoxide or amino groups available for covalently attaching protein molecules via reactive surface moieties.…”

Section: Introductionmentioning

confidence: 99%

Effect of pore size on the performance of immobilised enzymes

2013

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Porous materials are widely employed as supports in the immobilisation of enzymes. Traditionally macroporous materials with pore diameters >50 nm were believed to be the most suitable support material, ensuring no spatial restrictions upon enzyme molecules entering such large pores. In recent years however, there has been growing emphasis in the use of mesoporous supports with pore diameters ranging between 2 and 50 nm. It is thought this smaller pore range may offer enhanced conformational stability to immobilised enzymes while not being so small as to restrict enzyme access. Despite their increasing popularity, many argue that mesoporous materials have not yet proven superior to traditional macroporous supports for enzyme immobilisation. Through the design and application of a unique confidence rating system we were able to accurately compare data and establish trends between pore characteristics and protein loading. By analysing published data (182 experiments in total) and extracting pore characteristics and protein loading values, we have described three categories of pore diameters in which correlations between pore characteristics and protein loading are noted. With pore diameters less than 10 nm we see a general decrease in protein loading as the enzymes find physical restrictions in accessing the high surface offered in this pore diameter range. At pore sizes greater than 100 nm, protein loading generally decreases due to a concomitant reduction in available surface area. In the pore range of 10-100 nm there it is expected to see a decrease in protein loading level with increasing pore diameter. In fact protein loading in this range remains largely constant, suggesting some degree of protein-protein interaction blocking pores and restricting access to the increasing surface area available at decreasing pore diameters. No trends were established between pore characteristics and retention of activity.

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“…During earlier times, the enzyme immobilization or in-solubilization process was synonymously used ( Patel et al, 1969 ). The term “enzyme immobilization” refers to the physical confinement of the soluble proteinaceous enzyme molecules via different interactions to the carrier’s matrix in a region of space such as cross-linking/embedding, generally an insoluble material that can be easily removed from the medium, using simple basic procedures such as filtration, centrifugation, self-aggregation, or sieving ( Mosbach, 1976 ). The characteristics of immobilized enzymes are largely governed by four important factors in an enzyme immobilization process, which are the nature and type of enzyme employed, the nature of the carrier, and the immobilization conditions ( Datta et al, 2013 ; Liu et al, 2020 ).…”

Section: Immobilization Of Enzymes and Old Vs New Strategiesmentioning

confidence: 99%

An Insight in Developing Carrier-Free Immobilized Enzymes

Chauhan

Kaushal

Dhiman

et al. 2022

Front. Bioeng. Biotechnol.

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Enzymes play vital roles in all organisms. The enzymatic process is progressively at its peak, mainly for producing biochemical products with a higher value. The immobilization of enzymes can sometimes tremendously improve the outcome of biocatalytic processes, making the product(s) relatively pure and economical. Carrier-free immobilized enzymes can increase the yield of the product and the stability of the enzyme in biocatalysis. Immobilized enzymes are easier to purify. Due to these varied advantages, researchers are tempted to explore carrier-free methods used for the immobilization of enzymes. In this review article, we have discussed various aspects of enzyme immobilization, approaches followed to design a process used for immobilization of an enzyme and the advantages and disadvantages of various common processes used for enzyme immobilization.

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Immobilised enzymes

Cited by 58 publications

References 63 publications

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Effect of pore size on the performance of immobilised enzymes

An Insight in Developing Carrier-Free Immobilized Enzymes

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