Immobilization of glucoamylase and trypsin on crosslinked thermosensitive carriers

Hamerska-Dudra, Agnieszka; Bryjak, Jolanta; Trochimczuk, Andrzej W.

doi:10.1016/j.enzmictec.2007.01.008

Cited by 39 publications

(36 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Dudra et al immobilized trypsin on thermosensitive p(NIPAM-HEMA) copolymers forming an interpenetrated polymer network. The immobilization yield was 23.4% with retained activity lower than 35% [31]. Bryjak et al also compared different activation Fig.…”

Section: Presents Thementioning

confidence: 99%

A Novel Reversible pH-Triggered Release Immobilized Enzyme System

Gai

2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

A novel immobilized enzyme system supported by poly(acrylic acid/N,N'-methylene-bisacryl-amide) hydrogel microspheres was prepared. This system exhibited characteristics of reversible pH-triggered release. The morphology, size, and chemical structure were examined through optical microscopy, particle size analyzer, and Fourier transform infrared spectrometer. Immobilization and release features were further investigated under different conditions, including pH, time, and microsphere quantity. Results showed the microspheres were regularly spherical with 3.8 approximately 6.6 microm diameter. Loading efficiencies of bovine serum albumin immobilized by gel entrapment and adsorption methods were 93.9% and 56.2%, respectively. The pH-triggered protein release of the system occurred when medium pH was above 6.0, while it was hardly detected when medium pH was below 6.0. Release efficiencies of entrapped and adsorbed protein were 6.38% and 95.0%, respectively. Hence, adsorption method was used to immobilize trypsin. Loading efficiency of 77.2% was achieved at pH 4.0 in 1 h. Release efficiency of 91.6% was obtained under optimum pH catalysis condition set at 8.0 and trypsin was free in solutions with retention activity of 63.3%. And 51.5% of released trypsin could be reloaded in 10 min. The results indicate this kind of immobilized enzyme system offers a promising alternative for enzyme recovery in biotechnology.

show abstract

Section: Presents Thementioning

confidence: 99%

A Novel Reversible pH-Triggered Release Immobilized Enzyme System

Gai

2008

Appl Biochem Biotechnol

View full text Add to dashboard Cite

show abstract

“…Immobilized enzyme preparations are useful catalysts for industrial biotransformations [4,5]. Immobilization of enzymes through covalent attachment has also been demonstrated to induce higher resistance to temperature, denaturants, and organic solvents in several cases [6][7][8]; therefore it has become a hot topic studied by scholars. The carrier bonding of enzymes may produce alterations in their observed activity, specificity, or selectivity [9].…”

Section: Introductionmentioning

confidence: 99%

“…Currently, a large variety of matrixes have been used in immobilized glucoamylase [7,[12][13][14]. The enzymes are linked to an insoluble matrix by chemical bonds, which generally produce very stable derivatives in which enzyme leakage is prevented.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Cross-Linked Glucoamylase Aggregates Immobilization by Using Dextrin and Xanthan Gum as Protecting Agents

Jia

et al. 2016

Catalysts

View full text Add to dashboard Cite

Abstract:In this paper glucoamylase from Aspergillus niger was immobilized by using a modified version of cross-linked enzyme aggregates (CLEA). The co-aggregates were cross-linked with glutaraldehyde; meanwhile dextrin and xanthan gum as protecting agents were added, which provides high affinity with the enzyme molecules. The immobilized glucoamylase was stable over a broad range of pH (3.0-8.0) and temperature (55-75˝C); dependence shows more catalytic activity than a free enzyme. The thermostability, kinetic behavior, and first-order inactivation rate constant (k i ) were investigated. The two types of protector made the immobilized glucoamylase more robust than the free form. Both of the immobilized enzymes have excellent recyclability, retaining over 45% of the relative activity after 24 runs. In addition, immobilized enzymes reduced only 40% of the initial activity after three months by the storability measure, indicating high activity.

show abstract

“…Enzyme PSL was immobilized on the polymer pAA via covalent bonding. To accomplish this, pAA was first modified with aldehyde functional groups through reacting with GA . In a typical process, pAA (50 mg) and GA (9–57 mg) were stirred in deionized water (3 mL) at 45 °C for 6 h. Then the modified polymer, denoted as pAA‐GA, was separated by cooling precipitation and rinsed thoroughly with deionized water to remove unreacted GA.…”

Section: Methodsmentioning

confidence: 96%

Covalently Immobilized Lipase on a Thermoresponsive Polymer with an Upper Critical Solution Temperature as an Efficient and Recyclable Asymmetric Catalyst in Aqueous Media

Lou

et al. 2018

ChemCatChem

View full text Add to dashboard Cite

A thermoresponsive lipase catalyst with an upper critical solution temperature (UCST) of about 26 °C was exploited by covalent immobilization of an enzyme, Pseudomonas cepacia lipase (PSL), onto poly(acrylamide‐co‐acrylonitrile) by glutaraldehyde coupling. The experimental conditions for the PSL immobilization were optimized. The immobilized PSL was much more stable for wide ranges of temperature and pH than free PSL. The material was also evaluated as an asymmetric catalyst in the kinetic resolution of racemic α‐methylbenzyl butyrate at 55 °C in an aqueous medium and exhibited high catalytic performance and stability. Up to 50 % conversion and 99.5 % product enantiomeric excess were achieved, thus providing highly pure enantiomers. This biocatalyst could be easily recovered by simple decantation for reuse based on temperature‐induced precipitation. It showed good reusability and retained 80.5 % of its original activity with a well reserved enantioselectivity in the 6th cycle. This work would shed light on the future development of new UCST‐type enzyme catalysts.

show abstract

Immobilization of glucoamylase and trypsin on crosslinked thermosensitive carriers

Cited by 39 publications

References 23 publications

A Novel Reversible pH-Triggered Release Immobilized Enzyme System

A Novel Reversible pH-Triggered Release Immobilized Enzyme System

Preparation of Cross-Linked Glucoamylase Aggregates Immobilization by Using Dextrin and Xanthan Gum as Protecting Agents

Covalently Immobilized Lipase on a Thermoresponsive Polymer with an Upper Critical Solution Temperature as an Efficient and Recyclable Asymmetric Catalyst in Aqueous Media

Contact Info

Product

Resources

About