Agar–agar entrapment increases the stability of endo-β-1,4-xylanase for repeated biodegradation of xylan

Bibi, Zainab; Shahid, Faiza; Qader, Shah Ali Ul; Aman, Afsheen

doi:10.1016/j.ijbiomac.2014.12.051

Cited by 52 publications

(24 citation statements)

References 28 publications

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“…This shift in temperature optima might occur due to the impairment of hydrophobic and secondary interactions of the enzyme molecules within the matrix which improved at higher temperature to attain the maximum catalytic activity. It has been reported earlier that the immobilized endo-β-1,4-xylanase showed maximum relative activity at 60 °C which was 10 °C increase in temperature as compared to free enzyme [25] . Same finding was reported when endo (1→4) β- D -glucanase immobilized within agar–agar matrix using same technique where temperature optima was shifted from 60 °C to 70 °C after immobilization [26] .…”

Section: Resultsmentioning

confidence: 79%

Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Nawaz

Rehman

Bibi

et al. 2015

Biochemistry and Biophysics Reports

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Maltase from Bacillus licheniformis KIBGE-IB4 was immobilized within calcium alginate beads using entrapment technique. Immobilized maltase showed maximum immobilization yield with 4% sodium alginate and 0.2 M calcium chloride within 90.0 min of curing time. Entrapment increases the enzyme–substrate reaction time and temperature from 5.0 to 10.0 min and 45 °C to 50 °C, respectively as compared to its free counterpart. However, pH optima remained same for maltose hydrolysis. Diffusional limitation of substrate (maltose) caused a declined in Vmax of immobilized enzyme from 8411.0 to 4919.0 U ml−1 min−1 whereas, Km apparently increased from 1.71 to 3.17 mM ml−1. Immobilization also increased the stability of free maltase against a broad temperature range and enzyme retained 45% and 32% activity at 55 °C and 60 °C, respectively after 90.0 min. Immobilized enzyme also exhibited recycling efficiency more than six cycles and retained 17% of its initial activity even after 6th cycles. Immobilized enzyme showed relatively better storage stability at 4 °C and 30 °C after 60.0 days as compared to free enzyme.

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Section: Resultsmentioning

confidence: 79%

Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Nawaz

Rehman

Bibi

et al. 2015

Biochemistry and Biophysics Reports

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“…Thermal stability can be improved if endo-β-1,4-xylanase is immobilized on different matrices. Endo-β-1,4-xylanase from the same strain was immobilized within agar-agar matrix previously, and it relatively showed improved thermal stability as compared to calcium alginate environment (Bibi et al 2015). It is possible that elevated temperature may denature the catalytic function of an enzyme in the micro environment of the matrix used.…”

Section: Resultsmentioning

confidence: 99%

Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29

2015

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Exploration of microbial pool from extremely diversified ecosystem is significantly important for various industrial applications. Bacterial communities from extreme habitats including volcanic vents, hot springs, and industrial sectors are eagerly explored for the isolation of thermophiles. Geobacillus stearothermophilus KIBGE-IB29, isolated from blast furnace site of a steel processing industry, is capable of producing thermostable endo-β-1,4-xylanase. In the current study, this enzyme was immobilized within calcium alginate beads using entrapment technique. Amalgamation of sodium alginate (40.0 gL(-1)) and calcium chloride (0.4 M) was used for the formation of immobilized beads. It was observed that temperature (50 °C) and pH (7.0) optima of immobilized enzyme remained same, but enzyme-substrate reaction time increased from 5.0 to 30.0 min as compared to free enzyme. Diffusion limit of high molecular weight xylan (corncob) caused a decline in V max of immobilized enzyme from 4773 to 203.7 U min(-1), whereas K m value increased from 0.5074 to 0.5722 mg ml(-1) with reference to free enzyme. Immobilized endo-β-1,4-xylanase showed its stability even at high temperatures as compared to free enzyme and retained 18 and 9 % residual activity at 70 and 80 °C, respectively. Immobilized enzyme also exhibited sufficient recycling efficiency up to five reaction cycles which indicated that this enzyme can be a plausible candidate in paper and pulp industry.

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“…However, it may be very useful to prevent enzyme subunit dissociation of multimeric enzymes (Fernandez‐Lafuente ). Entrapment of enzymes is a simple technique of enzyme immobilization (Reetz and others ; Katiyar and Ali ; Bibi and others ; Biró and others ). However, it may hardly improve enzyme properties (exception is made on multimeric enzymes, preventing enzyme dissociation, or generation of favorable enzyme environments), and it tends to be not very simple to be performed at a large scale.…”

Section: Improving Proteases For Biotechnology Applicationsmentioning

confidence: 99%

Biotechnological Applications of Proteases in Food Technology

Tavano

Berenguer-Murcia

Secundo

et al. 2018

Comp Rev Food Sci Food Safe

235

105

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This review presents some of the hottest topics in biotechnological applications: proteases in biocatalysis. Obviously, one of the most relevant areas of application is in the hydrolysis of proteins in food technology, and that has led to a massive use on proteomics. The aim is to identify via peptide maps the different proteins obtained after a specific protease hydrolysis. However, concepts like degradomics are also taking on a more relevant importance in the use and study of proteases and will also be discussed. Other protease applications, as seem in cleaning (detergent development), the pharmaceutical industry, and in fine chemistry, will be analyzed. This review progresses from basic areas such as protease classification to a discussion of the preparation of protease-immobilized biocatalysts, considering the different problems raised by the use of immobilized proteases due to the peculiar features of the substrates, usually large macromolecules. Production of bioactive peptides via limited hydrolysis of proteins will occupy an important place in this review.

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Agar–agar entrapment increases the stability of endo-β-1,4-xylanase for repeated biodegradation of xylan

Cited by 52 publications

References 28 publications

Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29

Biotechnological Applications of Proteases in Food Technology

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