Alkaline phosphatase and pepsin immobilized in gels

Hirano, Seishiro; Miura, Osamu

doi:10.1002/bit.260210415

Cited by 30 publications

(9 citation statements)

References 16 publications

(2 reference statements)

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“…This observed change in optimum temperature was probably because of the restricted mobility of the immobilized enzyme, which is caused by the immobilization procedure. Similar results have been reported in other publications for the immobilization of enzymes onto chitosan polymer and chitosan nanoparticles (Hirano and Miur, 1979;Tang et al, 2006). …”

Section: Efficiency Of Enzyme Immobilizationsupporting

confidence: 92%

“…In contrast to the free enzyme, the immobilized enzyme does not show an optimum pH, but a maximum activity over the pH range 7.75-9.5. Similar results have been reported in the literature (Hirano and Miur, 1979;Tang et al, 2006). In addition, beta-glucosidase exhibited broader pH and temperature ranges when immobilized on chitosan beads using the crosslinking-adsorption-crosslinking method (Zhou et al, 2013).…”

Section: The Optimum Phsupporting

confidence: 86%

“…Determination of the binding efficiency indicated that 71% of the immobilized protein maintained its native activity. Similar investigations were performed by Hirano and Miur (1979) and Zubriene et al (2003). They used chitosan polymer and chitosan microparticles to immobilize alkaline phosphatase, respectively.…”

Section: Efficiency Of Enzyme Immobilizationsupporting

confidence: 82%

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Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Jafary

Panjehpour

Varshosaz

et al. 2016

Braz. J. Chem. Eng.

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-Enzyme engineering via immobilization techniques is a suitable approach for improving enzyme function and stability and is superior to the other chemical or biological methods. In this study chitosan nanoparticles were synthesized using the Ionic Gelation method and were characterized by Fourier Transform Infrared Spectroscopy (FTIR), Scanning Electron Microscopy (SEM) and Transmission Electron Microscopy (TEM). Alkaline phosphatase was successfully immobilized on the chitosan nanoparticles in optimum conditions. Chitosan nanoparticles were used because of their special properties for enzyme immobilization. This study indicated that the immobilized enzyme has improved function at high temperature and during storage. Immobilization resulted in an increased range of optimum pH and temperature, and reusability of enzyme. Furthermore, the binding efficiency calculation indicated that the immobilized alkaline phosphatase conserved 71% of its native activity. Kinetic parameter studies indicated no significant difference between the immobilized and free enzymes.

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Section: Efficiency Of Enzyme Immobilizationsupporting

confidence: 92%

Section: The Optimum Phsupporting

confidence: 86%

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Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Jafary

Panjehpour

Varshosaz

et al. 2016

Braz. J. Chem. Eng.

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“…Pepsin has been immobilized on a large number of supports by methods including covalent binding, crosslinking or copolymerization and it has been shown that immobilized pepsin was able to hydrolyse many proteins such as albumin (Hirano et al, 1979), serum albumin (Grubhofer and Schleith, 1954;Vretblad and Axen, 1971), haemoglobin (Goldstein, 1973;Valentova et al, 1975;AbdeI-Hay et al, 1980), casein (Puvanakrishnan and Bose, 1984;Findlay et al, 1986) or immunoglobulins (Tomono et al, 1981). However those studies were generally carried out in batch reactions and the stability of the enzyme was limited to the possibility of repeated uses in a short length of time or to the verification of enzyme activity after a long storage at low temperature.…”

Section: Introductionmentioning

confidence: 99%

Stabilization of pepsin on duolite for the continuous hydrolysis of bovine haemoglobin at pH2 and 40�C

Sannier¹,

Piot²,

Guillochon³

et al. 1993

Biotechnol Tech

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Several methods of pepsin immobilization have been applied in order to achieve the continuous hydrolysis of a 2,5% haemoglobin solution at pH 2 and 40°C. Methods using glutaraldehyde were unsuccesful because of the unstability of the derived enzyme at low pH. Pepsin covalently bounded to a Duolite amine resin by a carbodiimide showed a half life of 15 days during the hydrolysis of haemoglobin in a column reactor, No enzyme activity was detected in the hydrolysates. No accumulation of haem in the column was noticed which could have limited long term studies by plugging the system. Modulation of the degree of hydrolysis was also performed by changing the feeding flow rate of the reactor.

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“…Also, enzymes have been immobilized in or on chitosan using either physical (Stanley et al, 1976;Synowiecki et al, 1981;Nozawa et al, 1982) or covalent (Synowiecki et ai., 1982;Hirano and Miura, 1979;Iyengar and Rao, 1979;Yamaguchi et al, 1982;Carrara and Rubiolo, 1994;Itoyama et al, 1994) bonding. The method we used for covalently immobilizing the tyrosinases within the chitosan gels is illustrated in Figure 1, which shows that enzyme andglutaraldehyde were added to acidic chitosan solutions prior to forming the gel beads.…”

Section: Resultsmentioning

confidence: 96%

Tyrosinase Reaction/Chitosan Adsorption: Potential for Removing Polymerization Storage Inhibitors

Patel¹,

Sun²,

Payne³

1994

Ind. Eng. Chem. Res.

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Polymerization inhibitors are added to monomer solutions to prevent the inadvertent initiation of free radical polymerization during monomer storage and transportation. Residual levels of these inhibitors can be a source of irreproducibility in polymerization kinetics and can, therefore, disrupt efforts to control polymerization reactions for process optimization. We examined the feasibility of a non-capital-intensive separations approach for simply and efficiently removing the tertbutylcatechol storage inhibitor. The separations approach employs the enzyme tyrosinase to selectively oxidize the phenolic inhibitor, and the oxidation products are then strongly bound to a chitosan sorbent. For practicality we covalently immobilized the tyrosinase within chitosan gels to yield beads which served as both catalyst and sorbent for the phenolic inhibitor. These tyrosinasecontaining chitosan gels were shown to be capable of removing low levels of tert-butylcatechol from both aqueous and organic phases and thus have the potential to be exploited for removing phenolic inhibitors in a range of polymerization operations. The use of tyrosinase-containing chitosan gels for waste minimization is discussed.

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Alkaline phosphatase and pepsin immobilized in gels

Cited by 30 publications

References 16 publications

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Stabilization of pepsin on duolite for the continuous hydrolysis of bovine haemoglobin at pH2 and 40�C

Tyrosinase Reaction/Chitosan Adsorption: Potential for Removing Polymerization Storage Inhibitors

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