An active insoluble aggregate of <i>E. coli</i> β‐galactosidase

Khare, Sunil Kumar; Gupta, Munishwar N.

doi:10.1002/bit.260350113

Cited by 25 publications

(4 citation statements)

References 16 publications

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“…[14] The addition of BSA is proposed to enhance the formation of the reticulate, providing additional structure and preventing excessive crosslinking of catalytic enzyme. [15] Consistent with these observations, inclusion of BSA in the nucleotide generation pathway significantly enhanced stability in reuse studies. Particles generated with BSA retained up to 60 % of their original activity after seven uses (Figure 3 B).…”

supporting

confidence: 64%

Five‐Component Cascade Synthesis of Nucleotide Analogues in an Engineered Self‐Immobilized Enzyme Aggregate

Scism

Bachmann

2009

ChemBioChem

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supporting

confidence: 64%

Five‐Component Cascade Synthesis of Nucleotide Analogues in an Engineered Self‐Immobilized Enzyme Aggregate

Scism

Bachmann

2009

ChemBioChem

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“…Permeabilized Kluyveromyces fragilis cells have shown about 90% lactose hydrolysis in pasteurized skim milk within 1 h of treatment At a cell concentration of 1–2%, digitonin‐permeabilized yeast cells performed complete hydrolysis of the lactose present in milk within 2 h 7, 104. The immobilized E. coli enzyme resulted in 60% hydrolysis of lactose at 55 °C in 6 h, whereas, 45% hydrolysis was observed with native enzyme under similar conditions 105. The addition of Mg 2+ and Mn 2+ enhanced the hydrolysis of 2‐nitrophenyl β‐ D ‐galactopyranoside and lactose 106…”

Section: Applications Of β‐D‐galactosidasementioning

confidence: 98%

Microbial production, immobilization and applications of β‐D‐galactosidase

Panesar

Singh

et al. 2006

J of Chemical Tech & Biotech

237

158

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β-D-Galactosidase (β-D-galactoside galactohydrolase, E.C. 3.2.1.23), most commonly known as lactase, is one of the most important enzymes used in food processing, which catalyses the hydrolysis of lactose to its constituent monosaccharides, glucose and galactose. The enzyme has been isolated and purified from a wide range of microorganisms but most commonly used β-D-galactosidases are derived from yeasts and fungal sources. The major difference between yeast and fungal enzyme is the optimum pH for lactose hydrolysis. The application of β-D-galactosidase for lactose hydrolysis in milk and whey offers nutritional, technological and environmental applications to human life. In this review, the main emphasis has been given to elaborate the various techniques used in recent times for the production, purification, immobilization and applications of β-D-galactosidase.

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“…The lipase remained stable at 100°C for many hours, so did lysozyme. Such dramatic thermostabilization is seldom possible by using other approaches such as chemical crosslinking (Kamra and Gupta, 1988;Khare and Gupta, 1990;Rajput and Gupta, 1988), immobilization (Khare and Gupta, 1988 a,b) or even protein engineering (Nosoh and Sekiguchi, 1988). b) Apart from rigidity, another reason for enhanced thermostability is that a number of covalent processes involved in irreversible inactivation such as deamidation, peptide hydrolysis and cystine decomposition require water.…”

Section: Enhanced Thermostabititymentioning

confidence: 99%

Enzyme function in organic solvents

Gupta

1992

European Journal of Biochemistry

422

148

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Enzyme catalysis in organic solvents is being increasingly used for a variety of applications. Of special interest are the cases in which the medium is predominantly non-aqueous and contains little water. A display of enzyme activity, even in anhydrous solvents (water <0.02% by vol.), perhaps reflects that the minimum necessity for water is for forming bonds with polar amino acids on the enzyme surface.The rigidity of enzyme structure at such low water content results in novel substrate specificities, pH memory and the possibility of techniques such as molecular imprinting. Limited data indicates that, while enhanced thermal stability invariably results, the optimum temperature for catalysis may not change. If true in general, this enhanced thermostability would have extremely limited benefits.Medium engineering and biocatalyst engineering are relevant techniques to improve the efficiency and stability of enzymes in such low water systems. Most promising, as part of the latter, is the technique of protein engineering.Finally, this review provides illustrations of applications of such systems in the diverse areas of organic synthesis, analysis and polymer chemistry.For a classical biochemist, it was difficult to visualize enzymes catalyzing reactions in the absence of water, i.e. in non-aqueous media. Addition of organic solvents was done either to precipitate enzymes or to study denaturation. Thus, the study of enzyme action in organic solvents is a comparatively recent aspect of enzymology. Singer (1962) reviewed the status of this area and referred to it as a 'rapidly developing area of biophysical chemistry'. While we have made only limited advances since then in our understanding of biophysical chemistry of non-aqueous enzymology, its biotechnological implications have resulted in an explosive growth of the literature (Linhardt, 1986; Dordick, 1988).

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An active insoluble aggregate of E. coli β‐galactosidase

Cited by 25 publications

References 16 publications

Five‐Component Cascade Synthesis of Nucleotide Analogues in an Engineered Self‐Immobilized Enzyme Aggregate

Five‐Component Cascade Synthesis of Nucleotide Analogues in an Engineered Self‐Immobilized Enzyme Aggregate

Microbial production, immobilization and applications of β‐D‐galactosidase

Enzyme function in organic solvents

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