Basics of Enzyme Immobilization

Dwevedi, Alka

doi:10.1007/978-3-319-41418-8_2

Cited by 41 publications

(30 citation statements)

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“…The ZP hydrogels were loaded with subtilisin DY in order to impart a debridement function in relation to their planned application as wound dressings. Physical entrapment was chosen as a method for subtilisin DY loading into the ZP hydrogels as this method is simple, does not change the intrinsic enzyme properties and does not involve any chemical modification …”

Section: Resultsmentioning

confidence: 99%

“…Physical entrapment was chosen as a method for subtilisin DY loading into the ZP hydrogels as this method is simple, does not change the intrinsic enzyme properties and does not involve any chemical modification. 19 The subtilisin DY loading (entrapment) in pSBMA and pCBMA hydrogels was estimated in relation to their application as functional wound dressings (Fig. 4).…”

Section: Subtilisin Dy Loading In Zp Hydrogelsmentioning

confidence: 99%

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Polyzwitterionic hydrogels as wound dressings with enzymatic debridement functionality for highly exuding wounds

Ruseva

Nedkov

Alexandrova

et al. 2019

Polymer International

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Wound debridement is crucial for proper wound care as it promotes fast and efficient wound healing through removal of necrotic tissue. The latter not only impairs new healthy tissue formation but also increases the odour and the wound exudate, allowing bacteria and other harmful foreign invaders to spread and infect the wound. Hydrogel wound dressings are usually applied for promoting autolytic wound debridement but this is slow and not a very efficient process. On the other hand, enzymatic products for wound debridement are either ointments or gels and they are easily washed out when used for treating highly exuding wounds. This study is an attempt to combine enzymatic debridement functionality with the high swelling ability of polyzwitterionic networks and to produce an innovative dressing with debridement functionality for the healing of highly exuding wounds. For this purpose, two polyzwitterionic hydrogels were synthesized, poly(sulfobetaine methacrylate) and poly(carboxybetaine methacrylate) hydrogels, which were loaded with the protease subtilisin DY for imparting debridement functionality. The swelling ability and mechanical properties of zwitterionic polymer (ZP) hydrogels were shown to depend on their different propensities to physical network formation. Poly(carboxybetaine methacrylate) hydrogels demonstrated better capacity for wound exudate absorption as well as for exerting higher enzymatic debridement activity. Both ZP hydrogels were shown to be non‐cytotoxic which confirms their appropriateness for direct contact with injured tissues. Thus, the newly developed ZP hydrogels demonstrate the potential to be used as new dressing materials with enzymatic debridement functionality for highly exuding wounds. © 2019 The Authors. Polymer International published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 99%

Section: Subtilisin Dy Loading In Zp Hydrogelsmentioning

confidence: 99%

Polyzwitterionic hydrogels as wound dressings with enzymatic debridement functionality for highly exuding wounds

Ruseva

Nedkov

Alexandrova

et al. 2019

Polymer International

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Section: Cell and Enzyme Immobilization And Process Optimizationmentioning

confidence: 99%

“…The substrate molecules would be hindered from reacting with active site due to increased enzyme concentration at surface or inside of the matrix used for immobilization. This mechanism leads to constant reaction rates for longer duration despite variations in pH of the reaction mixture(Dwevedi, 2016).For food applications, polymers of biological origin are favored while simple methods and inexpensive supports are important for industrial applications. The enzyme immobilization methods using substrates such as micro porous sheets, glass beads, and carbon for packed bed reactors and alginate, cellulose acetate, and titanium dioxide for process applications may result in increased activity by providing a suitable microenvironment and better thermostability, and pH tolerance for the enzyme.…”

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confidence: 99%

β-galactosidase: Biotechnological applications in food processing

2018

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β‐Galactosidases produced by microorganisms are being used in food technology for hydrolysis of lactose in milk and milk by‐products. The enzyme has attracted much attention in view of lactose intolerance in human population and due to importance of milk in human diet. β‐Galactosidase hydrolyze β‐galactopyranosides, that is, lactose, and form a range of trans‐galactosylation products or galactooligosaccharides (GOS) capable of providing several health benefits as prebiotics. In addition, the enzyme also finds applications in production of lactose based sweeteners from high lactose containing effluents of cheese manufacturing industries. Currently, the enzyme is mainly obtained from Aspergillus niger and Kluyveromyces lactis, however, they are thermolabile with optimum pH between 4.0 and 6.0 accompanied by low chemical resistance and high product inhibition properties. Thermostable enzymes are suitable to perform the hydrolytic process at relatively high temperatures, minimizing pathogen contamination, psychrophilic β‐galactosidases are preferred for treatment of milk under refrigerated conditions (<15°C), without heating and maintenance of temperature. Lactic acid bacteria (LAB) are a potential source of food grade enzymes and other metabolites. Although reports on the use of β‐galactosidase of LAB in pure form is reported for hydrolysis of lactose in milk and production of fermented milk products for reduced lactose content, methods of immobilization for use in continuous bioreactors are less explored. Recombinant DNA technology has attained much significance to reveal molecular aspects of enzyme catalysis, protein structure, gene organization for expression, and enhancement of thermophilic, psychrophilic, and mesophilic β‐galactosidases. Heterologous expression of extremozymes with β‐galactosidase would help in overcoming the limitations faced within the bioprocess technology. Practical applications Lactic acid bacteria (LAB) producing extracellular cell bound β‐galactosidase have been isolated and enzyme production was carried out using modified MRS medium incorporating lactose as enzyme inducer. Process for growing probiotic lactic acid bacteria for β‐galactosidase from fermented milk products has been patented (Indian Patent No. 247904). Thermostable β‐galactosidases were also extracted from Kluyveromyces lactis a yeast, isolated from curd samples and Bacillus sp. MTCC 864. An Indian patent has been granted for a simple, cost effective perforated two compartment immobilized enzyme bioreactor was designed and fabricated for lactose hydrolysis (Indian Patent No. 264609). The bioreactor can be operated continuously at temperature between 5.0 and 75.0°C, employing different immobilized enzyme preparations for different operational temperatures. β‐galactosidase of cell confined LAB and yeast have been immobilized in agarose and galactooligosaccharides (GOS) production was observed at 40% lactose concentration in 0.05M phosphate buffer at pH 6.5. Immobilized bioreactor preparation could be used for lactos...

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“…The free and immobilised glucoaaylase used in the experiments were found to have the specific activity of 30.335.17 U g -1 and 1.856.78 U g -1 , respectively. The specific activity reduction after the immobilisation process was frequently found because conformational changes on enzyme structures occurred so that some active sites are difficult to be accesses by substrates [16,17].…”

Section: Immobilised Glucoamylasementioning

confidence: 99%

Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica

Agustian

Hermida

2018

Eurasian Chem. Tech. J.

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As insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be used to develop large-scale operations. The experiments gave dextrose equivalent (DE) values of 6.15–69.50% (w/w). Factors of pH and temperature affected the process highly. The suggested quadratic polynomial model is significant and considered acceptable (R2 = 99.78%). Justification of the model confirms its validity and adequacy where the predicted DE shows a good agreement with the experimental results. The kinetic constants (Vmax, KM) produced by the immobilised enzyme differed highly from the values yielded by free glucoamylase indicating reduction of substrate access to enzyme active sites had occurred.

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Basics of Enzyme Immobilization

Cited by 41 publications

References 0 publications

Polyzwitterionic hydrogels as wound dressings with enzymatic debridement functionality for highly exuding wounds

Polyzwitterionic hydrogels as wound dressings with enzymatic debridement functionality for highly exuding wounds

β-galactosidase: Biotechnological applications in food processing

Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica

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