Concanavalin A: A useful ligand for glycoenzyme immobilization—A review

Saleemuddin, M.; Husain, Qayyum

doi:10.1016/0141-0229(91)90146-2

Cited by 107 publications

(90 citation statements)

References 41 publications

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“…The use of low cost supports, such as alginate, gelatin, starches and agar is an important alternative to industrial use of immobilized enzymes. Nevertheless, these supports present limitations due to their low physical stability, which can be minimized with the use of crosslinking and linking agents, such as glutaraldehyde and concanavalin A (ConA) (HUSAIN & SALEEMUDDIN, 1986;SALEEMUDDIN & HUSAIN, 1991). Articles described in the literature have immobilized Aspergillus oryzae β-galactosidase using calcium alginate, gelatin and starch as supports, all treated with glutaraldehyde or ConA (HAIDER & HUSAIN, 2007;HAIDER & HUSAIN, 2009a;HAIDER & HUSAIN, 2009b;FREITAS et al, 2011).…”

Section: Food Technologymentioning

confidence: 99%

Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose

2016

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Section: Food Technologymentioning

confidence: 99%

Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose

2016

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“…The stabilization may also, result from the ''holding'' of the enzyme molecule at several places on the immunoaffinity supports, as has been suggested for several covalently immobilized enzymes (Blanco and Guisan, 1989) and glycoenzymes bound to con A supports (Iqbal and Saleemuddin, 1983b). Glutaraldehyde treatment may further the resistance to inactivation by restricting the unfolding process as a result of the introduction of both intra-and inter-molecular crosslinks, or by preventing the dissociation antibody glycoenzyme interactions as has been observed for lectin-glycoprotein interactions (Saleemuddin and Husain, 1991). Lateral interactions of the enzyme with antibody molecules closely positioned on the sepharose matrix may also confer additional stability to the enzyme (Sadana and Madgula, 1993).…”

Section: Resultsmentioning

confidence: 86%

“…Taking into consideration the high stability exhibited by invertase and several other glycoenzymes immobilized via their glycosyl residues (Saleemuddin and Husain, 1991), it is tempting to speculate that such sites may be located in the proximity of the glycosylation sites. In support of this, we have also observed recently that antiinvertase antibodies that bind to glycosyl residues confer significantly higher stability to the enzyme in the immunocomplexes than those that do not recognize the glycosyl residues (Jafri et al, 1995).…”

Section: Resultsmentioning

confidence: 99%

“…Among these, the affinity immobilization procedure employing the lectin concanavalin A (con A) appears to be the most promising (Saleemuddin and Husain, 1991). Several glycoenzymes however, do not bind or bind very weakly to con A, and the risk of desorption of those bound increases if the substrate/product of the enzyme is a carbohydrate with affinity for the lectin (Saleemuddin and Husain, 1991).…”

Section: Introductionmentioning

confidence: 98%

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Immobilization of invertase on sepharose-linked enzyme glycosyl recognizing polyclonal antibodies

Jafri

Saleemuddin

1997

Biotechnol. Bioeng.

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“…It is also nice to see Indian groups contributing to CLEA design. (Saleemuddin and Husain 1991;Saleemuddin 1999;Talekar et al, 2012) Use in low water media Very few groups work in this area. Parmar till recently had a group.…”

Section: Applied Bio-catalysis and "Make In India" Programmentioning

confidence: 99%

Skills in biocatalysis are essential for establishing a sound biotechnological base in India

Gupta¹

2015

Proceedings of the Indian National Science Academy

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Techniques developed by enzymologists and protein chemists have been indispensible in many areas of biotechnology. Bio-separation of proteins, biocatalyst engineering and medium engineering are important examples of this. Our understanding of enzyme specificity has helped us in gaining insight into catalytic promiscuity. This, along with the possibility of carrying out biocatalysis in organic solvents has widened the scope of using enzymes for organic synthesis.Reestablishing a strong base in enzymology is crucial towards creating a strong base for the field of biotechnology in India. Keywords IntroductionQuite a few aspects of biotechnology involve production and applications of enzymes. In the old days, most of these aspects were covered under industrial enzymology (Godfrey and Reichelt, 1983). Gradually, a more broad based term 'applied biocatalysis' came into vogue (Straathof and Adlercreutz, 2000) which was an interface between enzymology and biochemical engineering. This phase was characterized by few new developments: (1) As a result of the rDNA technology, our capability to produce mutant properties grew exponentially. There was a scramble to produce proteins at a lower cost. The stakes were no longer limited to low cost industrial grade enzymes. Costlier proteins used in molecular biology, diagnostics and biosensors and pharmaceutical proteins/enzymes could be produced by cloning and their properties tailored to suit the applications. The result was a paradigm shift in the downstream processing methods. Shorter and efficient protocols emerged. Affinity chromatography, rather than being a 'polishing' step at the end, was promoted to the earlier steps of purification. In fact, upstream and downstream processing steps were integrated (Gupta, 2002;Przybycien et al., 2004;Mondal et al., 2006). (2) It was realized that enzymes could be used in non aqueous media (Carrea and Riva 2000; Gupta 2000;Patel 2000; Vulfson et al., 2001). This opened up novel applications; especially in the synthesis of chiral compounds. Table 1 lists some of the milestones in the area of applied biocatalysis.It is remarkable how much enzymology contributed to all this.The present review attempts to emphasize the importance of the skills which are part of the toolbox Published Online on 10 December 2015 1114Munishwar Nath Gupta and Joyeeta Mukherjee et al., 1973; Mosbach 1976 Mosbach , 1980 Nilsson and Mosbach 1981; Mattiasson 1983;Mattiasson 1988) Berezin's group in Moscow was the third one (Berezin 1978; Mozhaev et al., 1987;Martinek and Mozhaev 1993). Current work is adequately discussed at many places ( Enzyme deactivation models Most people wrongly give half lives without analysing the kinetics of deactivation. Sadana's work needs to be known more widely. (Sadana 1991(Sadana , 1993 Enzymes as reverse micelles This is another approach in low water enzymology. (Luisi 1985; Larsson et al., 1987; Adlercreutz et al., 1988) Enzyme use in biosensors Immobilization allows enzymes to interface with transducers. (Yarapolov et al...

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Concanavalin A: A useful ligand for glycoenzyme immobilization—A review

Cited by 107 publications

References 41 publications

Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose

Kluyveromyces lactis β-galactosidase immobilization in calcium alginate spheres and gelatin for hydrolysis of cheese whey lactose

Immobilization of invertase on sepharose-linked enzyme glycosyl recognizing polyclonal antibodies

Skills in biocatalysis are essential for establishing a sound biotechnological base in India

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