Lipase from a Brazilian strain ofPenicillium citrinum

Abstract

A lipases (glycerol ester hydrolases E. C. 3.1.1.3) from a brazilian strain of Penicillium citrinum has been investigated. When the microorganism was cultured in the simple medium (1.0% olive oil and 0.5% yeast extract), using olive oil in as carbon source in the inocula, the enzyme extracted showed maximum activity (409 IU/mL). In addition, decrease of yeast extract concentration also reduces the lipase activity. Nevertheless, when yeast extract was replaced by ammonium sulfate, no activity was detected. Purification by precipitation with ammonium sulfate showed best activity in the 40-60% fraction. The optimum temperature for enzyme activity was found in the range of 34-37 degrees C. However, after 30 min at 60 degrees C, the enzyme was completely inactivated. The enzyme showed optimum at pH 8.0. The dried concentrated fraction (after dialysis and lyophilization) maintained its lipase activity at room temperature (28 degrees C) for 8 mo. This result in lipase stability suggests an application of lipases from P. citrinum in detergents and other products that require a high stability at room temperature.

Purification and Physicochemical Properties of Lipase from Thermophilic Bacillus aerius

“…This finding was in agreement with that of Al-Saleh and Zahran who showed that enzyme was produced in the absence of organic nitrogen by Pseudomonas flourescens 21 . In a similar study, Pimentel et al recorded that a Brazilian strain of Penicillium citrinum produced a maximal lipase activity of 409 IU/mL in a medium that contained yeast extract 0.5 as the nitrogen source and further decrease in yeast extract concentration reduced the attainable lipase activity also 22 .…”

Optimized production of lipase from Bacillus subtilis PCSIRNL-39

“…According to the work reported by Markossian et al (2000), B. thermoleovoraus showed maximum activity when yeast extract is used as nitrogen source. If the yeast extract is replaced by ammonium sulphate, no activity will be observed (Pimentel et al, 1994). Vmax and Km of PCSIRNL-39 lipase were measured to be 101 µmol/min/mL and 7.61 mg, whereas Vasiee et al (2016) reported Vmax and Km value of 0.367 μM/min/mL and 5.3 mM, respectively.…”

Partial Characterization of Proteases From Streptomyces Clavuligerus Using an Inexpensive Medium

“…The buffers used were citrate-phosphate (pH 5.0 -5.7, 0.1M), phosphate (pH 6.0 -8.0, 0.1M), and Tris-HCl (pH 7.2 -9.0, 0.2M) Pimentel et al (14).…”