Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 133, Issue -, Pages 8-14Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2017.02.010
Keywords
Collagenolytic enzyme; Collagen; ATPS; Purification
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Funding
- National Council of Technological and Scientific Development (CNPq)
- Coordination for the Improvement of Higher Education Personnel (CAPES)
- FCT [SFRH/BPD/88584/2012]
- Portuguese Science and Technology Foundation, Portugal [SFRH/BPD/88584/2012]
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Collagenases are proteolytic enzymes capable of degrading both native and denatured collagen, reported to be applied in industrial, medical and biotechnological sectors. Liquid-liquid extraction using aqueous two-phase system (ATPS) is one of the most promising bioseparation techniques, which can substitute difficult solid-liquid separation processes, offering many advantages over conventional methods including low-processing time, low-cost material and low-energy consumption. The collagenase produced by Penicillium sp. UCP 1286 showed a stronger affinity for the bottom salt-rich phase, where the highest levels of collagenolytic activity were observed at the center point runs, using 15.0% (w/w) PEG 3350 g/mol and 12.5% (w/w) phosphate salt at pH 7.0 and concentration. The enzyme was characterized by thermal stability, pH tolerance and effect of inhibitors, showing optimal collagenolytic activity at 37 degrees C and pH 9.0 and proved to be a serine protease. ATPS showed high efficiency in the collagenase purification, confirmed by a single band in SDS/PAGE, and can in fact be applied as a quick and inexpensive alternative method. (C) 2017 Elsevier Inc. All rights reserved.
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