Properties and enzymatic activities of papain insolubilized with glutaraldehyde

Jansen, Eugene F.; Olson, Alfred C.

doi:10.1016/0003-9861(69)90169-6

Cited by 72 publications

(20 citation statements)

References 16 publications

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“…135,136 However, intermolecular cross-linking of these biomolecules often results in low enzyme activity, poor reproducibility and low mechanical stability. 104,137 At the same time, the cross-linking of a crystalline enzyme via glutaraldehyde was reported, 138 eventually leading to a commercial immobilization technology called cross-linked enzyme crystals (CLECs or CLCs).…”

Section: C) Cross-linked Enzyme Aggregates (Cleas  )mentioning

confidence: 99%

Methods for stabilizing and activating enzymes in ionic liquids—a review

Zhao

2010

J of Chemical Tech & Biotech

339

241

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Ionic liquids (ILs) have evolved as a new type of non-aqueous solvents for biocatalysis, mainly due to their unique and tunable physical properties. A number of recent review papers have described a variety of enzymatic reactions conducted in IL solutions; on the other hand, it is important to systematically analyze methods that have been developed for stabilizing and activating enzymes in ILs. This review discusses the biocatalysis in ILs from two unique aspects (1) factors that impact the enzyme's activity and stability, (2) methods that have been adopted or developed to activate and/or stabilize enzymes in ionic media. Factors that may influence the catalytic performance of enzymes include IL polarity, hydrogen-bond basicity/anion nucleophilicity, IL network, ion kosmotropicity, viscosity, hydrophobicity, the enzyme dissolution, and surfactant effect. To improve the enzyme's activity and stability in ILs, major methods being explored include the enzyme immobilization (on solid support, sol-gel, or CLEA), physical or covalent attachment to PEG, rinsing with n-propanol methods (PREP and EPRP), water-in-IL microemulsions, IL coating, and the design of enzyme-compatible ionic solvents. It is exciting to notice that new ILs are being synthesized to be more compatible with enzymes. To utilize the full potential of ILs, it is necessary to further improve these methods for better enzyme compatibility. This is what has been accomplished in the field of biocatalysis in conventional organic solvents. c 2010 Society of Chemical Industry Keywords: ionic liquid; enzyme activity; enzyme stabilization; immobilization; biocatalysis NOTATION CationsBMIM + = 1-butyl-3-methylimidazolium C 2 OC 1 MIM + = 1-(2-methoxy)ethyl-3-methylimidazolium C 2 OHMIM + = 1-(2-hydroxy)ethyl-3-methylimidazolium EMIM + = 1-ethyl-3-methylimidazolium

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Section: C) Cross-linked Enzyme Aggregates (Cleas  )mentioning

confidence: 99%

Methods for stabilizing and activating enzymes in ionic liquids—a review

Zhao

2010

J of Chemical Tech & Biotech

339

241

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“…Clair and Navia, 1992), cross-linked enzymes (Habeeb, 1967;Jansen and Olson, 1969), and the recently developed methodology of cross-linked enzyme aggregates (CLEAs) (Cao et al, 2000). In this procedure, the enzyme is precipitated from an aqueous solution by adding a salt or a water-miscible organic solvent or polymer, such as poly (ethylene glycol).…”

Section: Introductionmentioning

confidence: 99%

A new, mild cross‐linking methodology to prepare cross‐linked enzyme aggregates

Mateo

Palomo

Langen

et al. 2004

Biotech & Bioengineering

272

165

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Cross-linked enzyme aggregates (CLEAs) were prepared from several enzymes (penicillin G acylase, hydroxynitrile lyase, alcohol dehydrogenase, and two different nitrilases) by precipitation and subsequent cross-linking using dextran polyaldehyde. In most cases, higher immobilization yields were obtained using the latter cross-linker as compared with the commonly used glutaraldehyde. Active site titration of penicillin acylase CLEAs showed that the higher activity originated from a significantly lower loss in active sites using dextran polyaldehyde as a cross-linking agent. It is proposed that macromolecular cross-linkers are too large to penetrate the protein active site and react with catalytically essential amino acid residues.

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“…This compound has some inherent properties that make it very appropriate for this type of measurement. Glutaraldehyde is very reactive against the N-terminal and e-amino group of lysine residues (but not with amino groups of Arg, Asn and Gln), 21 which are accessible in most proteins. Its low monomer mass, 82 or 64 Da, depending on whether one or both of the aldehyde groups have reacted, results in a relatively low increase in the molecular mass of the protein under study.…”

Section: Discussionmentioning

confidence: 99%

Analysis of the multimeric state of proteins by matrix assisted laser desorption/ionization mass spectrometry after cross-linking with glutaraldehyde

Helin¹,

Caldentey²,

Kalkkinen³

et al. 1999

Rapid Commun. Mass Spectrom.

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We have undertaken a systematic study on the suitability of matrix-assisted laser desorption/ionization mass spectrometry to analyze and determine the multimericity of several proteins after cross-linking with glutaraldehyde. Using both commercially available proteins and others of viral origin currently being characterized in our laboratory, we studied the range of concentrations of cross-linker and protein for optimal analysis. Under the conditions developed during this study, we confirmed the multimeric states of three phage PRD1 structural proteins with monomeric masses ranging from 13.5 to 63 kDa. In addition, we addressed the question of the general applicability of the method by using it successfully to confirm the stoichiometry of the heptameric chaperonin GroEL, a bacterial protein with a mass well over 450 kDa.

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Properties and enzymatic activities of papain insolubilized with glutaraldehyde

Cited by 72 publications

References 16 publications

Methods for stabilizing and activating enzymes in ionic liquids—a review

Methods for stabilizing and activating enzymes in ionic liquids—a review

A new, mild cross‐linking methodology to prepare cross‐linked enzyme aggregates

Analysis of the multimeric state of proteins by matrix assisted laser desorption/ionization mass spectrometry after cross-linking with glutaraldehyde

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