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One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite

Authorized Users Only
2012
Authors
Dimitrijević, Aleksandra
Veličković, Dušan
Bihelović, Filip
Bezbradica, Dejan
Jankov, Ratko M.
Milosavić, Nenad
Article (Published version)
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Abstract
Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect. (C) 2011 Elsevier Ltd. All rights reserved.
Keywords:
Candida antarctica / Lipase / Isolation / Purification / Hydroxyapatite
Source:
Bioresource Technology, 2012, 107, 358-362
Publisher:
  • Elsevier Sci Ltd, Oxford
Projects:
  • Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-172049)
  • Novel encapsulation and enzyme technologies for designing of new biocatalysts and biologically active compounds targeting enhancement of food quality, safety and competitiveness (RS-46010)
  • Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)

DOI: 10.1016/j.biortech.2011.11.077

ISSN: 0960-8524

PubMed: 22209131

WoS: 000301620600050

Scopus: 2-s2.0-84856573973
[ Google Scholar ]
18
14
URI
http://cherry.chem.bg.ac.rs/handle/123456789/1264
Collections
  • Publikacije
Institution
Hemijski fakultet
TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko M.
AU  - Milosavić, Nenad
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1264
AB  - Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite
VL  - 107
SP  - 358
EP  - 362
DO  - 10.1016/j.biortech.2011.11.077
ER  - 
@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Bihelović, Filip and Bezbradica, Dejan and Jankov, Ratko M. and Milosavić, Nenad",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1264",
abstract = "Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite",
volume = "107",
pages = "358-362",
doi = "10.1016/j.biortech.2011.11.077"
}
Dimitrijević A, Veličković D, Bihelović F, Bezbradica D, Jankov RM, Milosavić N. One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite. Bioresource Technology. 2012;107:358-362
Dimitrijević, A., Veličković, D., Bihelović, F., Bezbradica, D., Jankov, R. M.,& Milosavić, N. (2012). One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite.
Bioresource TechnologyElsevier Sci Ltd, Oxford., 107, 358-362.
https://doi.org/10.1016/j.biortech.2011.11.077
Dimitrijević Aleksandra, Veličković Dušan, Bihelović Filip, Bezbradica Dejan, Jankov Ratko M., Milosavić Nenad, "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite" 107 (2012):358-362,
https://doi.org/10.1016/j.biortech.2011.11.077 .

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