Immobilization of α-amylase on zirconia: A heterogeneous biocatalyst for starch hydrolysis

Reshmi, R.; Gopinath, Sanjay; Sugunan, S.

doi:10.1016/j.catcom.2006.07.009

Cited by 116 publications

(60 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Zirconia, a white crystalline solid with a high melting point and high chemical resistance, is also an attractive for the enzyme immobilization, where it is used in the form of nanoparticles , layered c-zirconium phosphate (Geng et al 2003) and as pure zirconium (Reshmi et al 2007). In addition to the above-mentioned materials, also alumina gel (Gupta and Prabhu 1995) and aluminium (Reshmi et al 2006) were tested as the enzyme carriers.…”

Section: Inorganic Carriersmentioning

confidence: 99%

“…Interestingly, laccase shows an affinity to organic carriers, which is considerably higher comparing to the inorganic carriers. In this context it was immobilized on chitosan membrane (Reshmi et al 2007), cellulose acetate disc membranes (Labus et al 2012) and commercial cationic resin Amberlite IR-120H (Spinelli et al 2012). Among inorganic carriers, the enzyme was immobilized on different silicas (Tavares et al 2013), e.g.…”

Section: Immobilized Enzymesmentioning

confidence: 99%

See 1 more Smart Citation

Enzyme immobilization by adsorption: a review

2014

View full text Add to dashboard Cite

Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes' low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.

show abstract

Section: Inorganic Carriersmentioning

confidence: 99%

Section: Immobilized Enzymesmentioning

confidence: 99%

Enzyme immobilization by adsorption: a review

2014

View full text Add to dashboard Cite

show abstract

“…Some previous researches performed with immobilization and chemical modification have shown that the enzymes obtained have significantly increased their stability against pH and temperature compared to the native enzyme (Yandri, et al, 2008(Yandri, et al, , 2010a(Yandri, et al, , 2010bGermain dan Crichton, 1988;Cordt, et al, 1992;Steadman, et al, 1991;Skerker dan Clark, 1987;Rani, et al, 2007;Reshmi, et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Yandri¹,

Susanti²,

Suhartati³

et al. 2012

MAS

View full text Add to dashboard Cite

This paper describes the stability increase of α-amylase obtained from Bacillus subtilis ITBCCB 148 by immobilization process using carboxymethyl cellulose (CM-Cellulose) as the immobile matrix. To achieve this aim the enzyme was purified by the following steps: fractionation with ammonium sulphate, dialysis, ion exchange column chromatography with CM-cellulose and molecule filtration column chromatography with Sephadex G-100. The purified enzyme was then immobilized with CM-Cellulose. The result showed that the immobilization with CM-cellulose on α-amylase obtained from B. subtilis has successfully increased the thermal stability of the native enzyme. The thermal stabilities of the modified enzyme were increased 3.67 times compared to the native enzyme. The decrease of ki value, the increase of half-life and ΔGi values showed that the modified enzymes were more stable than the native enzyme.

show abstract

“…Organic polymers, such as agarose are widely used in enzyme immobilization due to the abundance of functional groups on their surfaces capable of interacting with enzymes (Reshmi et al 2007). Agarose gels contain reactive hydroxyl groups, which can react with glutaraldehyde to form aldehydes.…”

Section: Introductionmentioning

confidence: 99%

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Nwagu

Okolo

Aoyagi

2011

World J Microbiol Biotechnol

View full text Add to dashboard Cite

Applications of raw starch digesting amylases (RSDAs) are limited due to instability, product inhibition of enzyme and contamination. RSDA from Aspergillus carbonarius was stabilized through immobilization on agarose gel by adsorption, spontaneous crosslinking and conjugation using glycidol, glutaraldehyde or polyglutaraldehyde. Effects of immobilization on kinetics, catalytic, storage and operational stability of immobilized enzyme were evaluated. Polyglutaraldehyde activated agarose RSDA (PGAg-RSDA) gave the highest immobilization yield (100%) with expressed activity of 86.7% while that of glycidol activated RSDA (GlyAg-RSDA) was 80.4%. A shift in pH from optimum of 5 for the soluble enzyme to 6 for RSDA adsorbed on agarose followed by crosslinking with glutaraldehyde (AgRSDA-CROSS) and simultaneous adsorption and crosslinking (AgRSDA-RET), and pH 7 for PGAg-RSDA was seen. PGAg-RSDA and AgRSDA-CROSS were most pH stable and retained over 82% of their activities between pH 3.5 and 9 compared to 59% for the soluble enzyme. Thermoinactivation studies showed that immobilized RSDAs with the exception of GAg-RSDA retained over 90% of their activities at 60°C for 120 min while soluble enzyme retained only 76% activity under the same condition. AgRSDA-CROSS, PGAg-RSDA, Gly-RSDA and GAg-RSDA retained approximately 100% of their activities after 30 days storage at 4°C. GlyAg-RSDA retained 99.6%, PGAg-RSDA 94%, AgRSDA-CROSS 90%, GAg-RSDA 86.5% and Ag-RSDA-RET 80% activity after 10 batch reactions. Immobilization stabilized RSDA and permits processing at higher temperatures to reduce contamination.

show abstract

Immobilization of α-amylase on zirconia: A heterogeneous biocatalyst for starch hydrolysis

Cited by 116 publications

References 30 publications

Enzyme immobilization by adsorption: a review

Enzyme immobilization by adsorption: a review

Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Contact Info

Product

Resources

About