A novel cold-adapted phospholipase A1 from Serratia sp. xjF1: Gene cloning, expression and characterization

Optimization of catalase production and purification and characterization of a novel cold-adapted Cat-2 from mesophilic bacterium Serratia marcescens SYBC-01

“…Although Serratia marcescens is a ubiquitous Gram-negative bacterium which is capable of causing disease in diverse organisms, including humans (Richards et al 2000), coral (Patterson et al 2002), insects (Adamo 2004), and plants (Pair et al 2004), it has also been applied in fermentation for the production of keratin hydrolyzing enzyme (Khardenavis et al 2009), protease (Romero et al 2001), phospholipase (Fu et al 2008), and chitinase (Duzhak et al 2002).…”

Degumming of ramie bast fibers by Ca2+-activated composite enzyme

“…Fu et al (2008) showed that activity of cold-adapted phospholipase A 1 (PLA 1 ) from a psychrotrophic, glacier soil bacterium Serratia sp. xjF1 could be slightly activated by Ca 2+ (Fu et al, 2008).…”

“…Fu et al (2008) showed that activity of cold-adapted phospholipase A 1 (PLA 1 ) from a psychrotrophic, glacier soil bacterium Serratia sp. xjF1 could be slightly activated by Ca 2+ (Fu et al, 2008). Schofield, Patchett, and Parker (2004) also mentioned that enzyme activity is restored by a wide range of divalent metal ions including (in order of decreasing effectiveness): Zn 2+ , Cd 2+ , Mn 2+ , Co 2+ , Ni 2+ , Ca 2+ , Hg 2+ , and Cu 2+ (Schofield, Patchett, & Parker, 2004).…”

Purification, Characterization and Application of a Cold- Adapted Phospholipase A1 fromBacillus Cereus Sp.AF-1

“…above 45 °C (5,8,19,20,23). The ability to work efficiently at low temperatures is environmentally advantageous and energy saving (7). Although several phospholipases isolated from Bacillus cereus which perform efficiently at lower temperature (below 40 °C) have been described (9,15,18,21), the reports do not discuss the properties of these enzymes, other than the low temperature of action and the processes used for effective purification.…”

“…These enzymes are widespread in nature and are both intra-and extra-cellular in origin (26). Fu et al (7) and Hartmann et al (10) determined the positional specificity of phospholipase by the hole around the colonies on lecithin-containing agar plates. Phospholipase A1 and phospholipase A2 both formed the same type of halo on the agar plates and were, therefore, not clearly distinguished by this method.…”