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090			_aB-20615
245	1	0	_aRecombinant Protein Production and Purification of Insoluble Proteins
490	0		_vMethods and Protocols, 2406, p.1-31, 2022
520	3		_aProteins are synthesized in heterologous systems because of the impossibility to obtain satisfactory yields from natural sources. The efficient production of soluble and functional recombinant proteins is among the main goals in the biotechnological field. In this context, it is important to point out that under stress conditions, protein folding machinery is saturated and this promotes protein misfolding and, consequently, protein aggregation. Thus, the selection of the optimal expression organism and its growth conditions to minimize the formation of insoluble protein aggregates should be done according to the protein characteristics and downstream requirements. Escherichia coli is the most popular recombinant protein expression system despite the great development achieved so far by eukaryotic expression systems. Besides, other prokaryotic expression systems, such as lactic acid bacteria and psychrophilic bacteria, are gaining interest in this field. However, it is worth mentioning that prokaryotic expression system poses, in many cases, severe restrictions for a successful heterologous protein production. Thus, eukaryotic systems such as mammalian cells, insect cells, yeast, filamentous fungus, and microalgae are an interesting alternative for the production of these difficult-to-express proteins.
650	1	4	_aAGGREGATION
650	1	4	_aHETEROLOGOUS SYSTEM
650	1	4	_aINSOLUBLE PROTEINS
650	1	4	_aPROTEIN EXPRESSION
650	1	4	_aPROTEIN PURIFICATION
650	1	4	_aRECOMBINANT PROTEINS
650	1	4	_aSOLUBILITY
700	1	2	_aFerrer-Miralles, N.
700	1	2	_aSaccardo, P.
700	1	2	_aCorchero, J. L.
700	1	2	_aGarcia-Fruitós, E.
856	4	0	_uhttps://drive.google.com/file/d/11eBVLfQm8wvwPkW2dfhv2S8ACVEmkQGy/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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