Adaptation, production, and biotechnological potential of cold-adapted proteases from psychrophiles and psychrotrophs: recent overview

Journal of Genetic Engineering and Biotechnology

Table 3 Molecular weight and purification of cold-adapted proteases (published from 2010 onwards)

Microbial source	Molecular weight	Chromatographic techniques	Purification fold/final yield	Reference
Acinetobacter sp.	35	DEAE cellulose and Sephacryl S-200	9.8/0.16	[63]
Bacillus sp.	62	Nm	3.82/76	[34]
Bacillus subtilis	38	DEAE cellulose	49.22/29.28	[30]
Halobacillus sp.	35	DEAEeSephadex, ion exchange, and Sephadex G-75 gel filtration	3077 ± 49/26	[37]
Lysobacter sp.	35	Nm	2.40/95.6	[18]
Planococcus sp.	35.6	His-Bind resin affinity chromatography	Nm	[23]
Planococcus sp.	43	DEAE-Sepharose	Nm	[60]
Penicillium nalgiovense	45.2	Nm	12.1/82.9	[40]
Pseudomonas lundensis	46	Gel filtration	14/20	[19]
Pseudomonas aeruginosa	32.8	DEAE-Sepharose and Sephacryl S-200 gel filtration	10/60	[21]
Pseudoalteromonas sp.	34.6	Affinity chromatography	Nm	[16]
Serratia marcescens	56	DEAE cellulose Fraction	9.9/51	[27]
Sporobolomyces roseus	31	HiTrap SPFF, Superose 12 and Mono S	103/25	[31]
Stenotrophomonas sp.	55	DEAE-Sepharose	18.45/47	[28]
Stenotrophomonas maltophilia	75	DEAE cellulose column	Nm	[29]