SciELO - Scientific Electronic Library Online

 
vol.30 issue2High-level production and aggregation of hepatitis B surface antigen in transgenic tobacco seedsZea mays L. plant growth promotion by Tsukamurella paurometabola strain C-924 author indexsubject indexarticles search
Home Pagealphabetic serial listing  

Services on Demand

Journal

Article

Indicators

  • Have no cited articlesCited by SciELO

Related links

  • Have no similar articlesSimilars in SciELO

Share


Biotecnología Aplicada

On-line version ISSN 1027-2852

Abstract

RAMIREZ, Hector L; BRIONES, Ana I; UBEDA, Juan  and  AREVALO, María. Immobilization of pectinase by adsorption on an alginate-coated chitin support. Biotecnol Apl [online]. 2013, vol.30, n.2, pp.101-104. ISSN 1027-2852.

Aspergillus niger pectinase was immobilized on an alginate-coated chitin support by adsorption. The optimal conditions for immobilization were: pH 4.5, time of incubation 2 h and 85 µg/mL protein concentration. The yield of immobilized protein was 70 % and the enzyme retained 60 % of the initial activity. Optimal pH, heat stability and reusability were evaluated, among other properties of the immobilized enzyme. The thermostability was enhanced by about 9.7 °C after immobilization. The immobilized pectinase was resistant during incubation, 10-fold more resistant to thermal treatment at 50 ºC than the native enzyme. The optimal pH for the catalytic activity of both, the immobilized pectinase and the free enzyme, was the same, the prepared biocatalyst retaining 50 % of the original catalytic activity after 9 cycles of reuse. The obtained bioconjugate showed good operational stability and improved thermostability. These properties support the potential application of the immobilized pectinase at the juices industry.

Keywords : pectinase; adsorption; chitin; alginate; enzyme stability; enzyme immobilization.

        · abstract in Spanish     · text in English     · English ( pdf )