Extraction and three-phase partitioning behavior of proteases from papaya peels

Autor:	Phanuphong Chaiwut, Punyawatt Pintathong, Saroat Rawdkuen
Rok vydání:	2010
Předmět:	chemistry.chemical_classification Proteases Chromatography biology Butanol Phosphate buffered saline Extraction (chemistry) Bioengineering Applied Microbiology and Biotechnology Biochemistry Enzyme assay chemistry.chemical_compound Enzyme chemistry biology.protein
Zdroj:	Process Biochemistry. 45:1172-1175
ISSN:	1359-5113
DOI:	10.1016/j.procbio.2010.03.019
Popis:	Dried papaya peels exhibited superior proteolytic activity to the fresh peels. An extraction with phosphate buffer pH 7.0 greatly maintained proteolytic activity when compared to water. SDS-PAGE verified that the extracted dried papaya peels held a wide range of proteins. To optimize the three-phase partitioning (TPP) for isolating the papaya peel proteases required a ratio of crude extract to t -butanol, the (NH 4 ) 2 SO 4 concentration and the TPP cycles. The ratio of the crude extract to t -butanol of 1.0:0.5 with the presence of 20% (NH 4 ) 2 SO 4 resulted in the highest proteolytic recovery at 253.5%, and 15.8-fold of purification in the bottom phase. The TPP was then optimized by adding up to 55% (NH 4 ) 2 SO 4 to the bottom phase of the first step. A purification of 10.1-fold with about 89.4% recovery was obtained. This study showed the TPP can be effectively employed for the extraction of proteases from papaya peels.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5fb0e358d170e3b7c26eb5ce2e56a761 https://doi.org/10.1016/j.procbio.2010.03.019 Zobrazit plný text záznamu Full Text from ScienceDirect