Preparation of Chitosan Beads for Trypsin Immobilization

Kamburov, M.; Lalov, Ivo

doi:10.5504/50yrtimb.2011.0029

Cited by 25 publications

(15 citation statements)

References 36 publications

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“…Egwim et al (2012) reported that lipase immobilized onto chitosan beads had improved thermal, operational and storage stabilities. In a study performed by Kamburov et al (2011) on covalent immobilization of trypsin on chitosan macrobeads, immobilization led to the increase of the enzyme heat resistance. Adriano et al (2005) indicated that the immobilization of penicillin G on chitosan activated by glutaraldehyde can increase the stability of the enzyme 4.9-fold at 50 °C and 4.5-fold at pH 10.0.…”

Section: Effect Of Temperature On Enzyme Stabilitymentioning

confidence: 99%

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: Effect Of Temperature On Enzyme Stabilitymentioning

confidence: 99%

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Jafary

Panjehpour

Varshosaz

et al. 2016

Braz. J. Chem. Eng.

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“…A quantity (2.5 g) of chitosan was dissolved in 1% acetic (100 mL) and concentrated at 75 °C until a chitosan hydrogel was formed as described by Kamburov and Lalov. 36 To form the macrobeads, the chitosan hydrogel was introduced as droplets into 30% sodium hydroxide (100 mL). The chitosan beads produced were then washed to neutrality and oven-dried overnight at 60 °C.…”

Section: Preparation Of the Chitosan Beadsmentioning

confidence: 99%

Immobilization of Lactobacillus acidophilus β-galactosidase on chitosan obtained from the shells of the African giant snail, Achatina achatina

2024

TJNPR

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Most GOS are classified as prebiotic food (since they are nondigestible) or Bifidus growth factor as they can stimulate the establishment of human colonic Bifidobacteria species. In addition, GOS, by suppressing the expression of bacterial quorum-sensing (QS) genes, could prevent the growth and production of biofilms by some possible harmful enteric bacteria. [10][11][12][13] Industrial β-galactosidases are usually sourced from microorganisms, especially fungi, bacteria, and yeasts. 8,9,14 Although many bacteria produce β-galactosidases, major β-galactosidase production has majorly focused on the use of some Lactobacillus species of the Lactic acid bacteria (LBA) with the "Generally Regarded As Safe (GRAS)" status. 15,16 LBA is naturally found in any environment rich in carbohydrates, such as decomposing plant materials, fermented foods, and in the feces of individuals on high milk, lactose, or dextrin diets. 17 Lactobacillus acidophilus ('acid-loving milk-bacillus') is a homofermentative species of Lactobacillus that grows at pH below 5.0 in the lumen of the gut, especially the lower end of the small intestine where it metabolizes any residual lactose, thus encouraging lactose digestion in individuals with low galactosidase activity. 15 Good thermostability and cost are major factors to consider in the industrial application of enzymes. 18 At higher temperatures, thermostable enzymes have increased activity, substrates maintain higher solubility and microbial fouling could be considerably reduced. 9 High cost is a critical issue in the industrial use of immobilized enzymes in relation to enzyme reusability and the regenerability of immobilization supports. This issue has been sufficiently addressed by the overwhelming choice of biopolymeric immobilization supports like some proteins and carbohydrates, but more especially the polysaccharides, chitin, and chitosan. [19][20][21] Chitin is one of the most abundant natural polymers. It can be easily obtained at a relatively low

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“…The presence of reactive amino groups CHS makes it a potential candidate for enzyme binding. CHS increases the free amino group concentration available for cross-linking, thus preventing the denaturation of the targeted trypsin enzyme and mediating a substantial cross-linking with retention of high enzymatic activity (Kamburov and Lalov, 2012;Li et al, 2018). For CHS, the cross-linking reaction occurs at a higher rate at pH > 6.5 when the CHS NH 2 groups are deprotonated.…”

Section: Preparation Of Trypsin Cleasmentioning

confidence: 99%

“…For CHS, the cross-linking reaction occurs at a higher rate at pH > 6.5 when the CHS NH 2 groups are deprotonated. Glutaraldehyde acts as an amino-fixing arm, forming covalent imine bonds with the amino groups, both in CHS and trypsin (Kamburov and Lalov, 2012;Sun et al, 2017).…”

Section: Preparation Of Trypsin Cleasmentioning

confidence: 99%

Bio-inspired trypsin-chitosan cross-linked enzyme aggregates: a versatile approach for stabilization through carrier-free immobilization

Mageed

Ezz

Radwan

2019

bta

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Enzymes are versatile catalysts for numerous industrial biocatalytic processes. Cross-linked enzyme aggregates (CLEAs) as a carrier free immobilization approach has drawn much attention being simple, cost efficient, capable of preserving high catalytic efficiency and improve enzyme reusability. The aim of this study was to develop a reusable, thermally and operationally stable trypsin CLEAs through co-aggregation with chitosan (CHS). Physicochemical characterization of the prepared CLEAs, including pH and temperature optimum, kinetic parameters, and operational and thermal stability in the absence (CLEA-T), and presence (CLEA-T-CHS) of CHS was carried out. CLEA-T-CHS and CLEA-T were prepared under mild conditions and cross linked using glutaraldehyde with 92% and 31% residual activity, respectively. Immobilized trypsin showed improved pH stability at alkaline pH. At 70EC the immobilized enzyme had 62% residual activity while the free enzyme lost 91% of its initial activity.The kinetic parameters (K m and V max ) of the immobilized trypsin marginally increased, leading to a decreased catalytic efficiency. Operational and thermal stability were highly improved for CLEA-T-CHS; the half-life (t 1/2 ) of free trypsin and CLEA-T-CHS were 15 min and 65 min, respectively. Storage stability was highly improved; CLEA-T-CHS and the free enzyme had 82% and 21% residual activity, respectively, after storage for 4 weeks. CLEA-T-CHS retained 64% residual activity after five consecutive hydrolytic cycles, thus reinforcing its robust potentials. In this study, we successfully prepared a thermally stable and highly active immobilized trypsin through crosslinking in the presence of CHS. Results suggest that CLEA-T-CHS has great potential for industrial applications, including re-use in protein digestion.

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Preparation of Chitosan Beads for Trypsin Immobilization

Cited by 25 publications

References 36 publications

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Immobilization of Lactobacillus acidophilus β-galactosidase on chitosan obtained from the shells of the African giant snail, Achatina achatina

Bio-inspired trypsin-chitosan cross-linked enzyme aggregates: a versatile approach for stabilization through carrier-free immobilization

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