Antioxydant activity, oxidative stability properties of Colza oil, comparison of mechanical agitated and ultrasonic extraction on green tea catechins of Camellia sinensis L.

peer reviewedUltrasonic extraction “UE” used to optimize the extraction yield of phenolic compounds “PC” from green tea Camellia sinensis L., and compared with mechanical agitated extraction “MAE”. UE was applied at different times (15, 10 and 5min) and temperatures (25, 60 and 95°C) and MAE was performed at these experimental conditions (15 min, 95°C, 400 rpm). Results demonstrate that the maximum yield of epigallocatechin 3-gallate “EGCG” extracted by UE was significantly (P < 0.05) higher than that obteined using MAE (136 mg/g vs 100 mg/g, respectively). The optimum conditions for the polyphenol compounds “PC” recovery are obtained using UE during 15 min at 95°C (~134.66 mg/g). Four catechins from extracted PC were identified using high-performance liquid chromatography equipped with a diode array detector and liquid chromatography mass spectrometry “HPLC-DAD & LC-MS”: epigallocatechin “EGC”, epicatechin “EC”, epigallocatechingallate “EGCG”, and epicatechin-gallate “ECG”. EGCG is the major compound in polyphenol extracts representing 60 %. The antioxidant capacity of the obtained extracts was also studied. Diphényl-2-pycril-hydrazyl “DPPH” scavenging activity is higher for UE than MAE (~ 90 % vs ~85%). Moreover, the PC obtained by UE added to colza oil had a higher oxidative stability, determined by rancimat than those extracted by MAE method (~30.62 h vs ~21.26 h). Results indicate the suitability of UE method for production of PC as potent antioxidant for stabilization of vegetable oils such as colza oil

Biochemical characterization of a detergent-stable serine alkaline protease from Caldicoprobacter guelmensis

Caldicoprobacter guelmensis isolated from the hydrothermal hot spring of Guelma (Algeria) produced high amounts of extracellular thermostable serine alkaline protease (called SAPCG) (23,000 U/mL). The latter was purified by ammonium sulphate precipitation, UNO Q-6 FPLC and Zorbex PSM 300 HPLC, and submitted to biochemical characterization assays. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme was a monomer, with a molecular mass of 55,824.19 Da. The 19 N-terminal residue sequence of SAPCG showed high homology with those of microbial proteases. The enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP), which suggested its belonging to the serine protease family. It showed optimum protease activity at pH 10 and 70 degrees C with casein as a substrate. The thermoactivity and thermostability of SAPCG were enhanced in the presence of 2 mM Ca2+. Its half-life times at 80 and 90 degrees C were 180 and 60 min, respectively. Interestingly, the SAPCG protease exhibited significant compatibility with iSiS and Persil, and wash performance analysis revealed that it could remove bloodstains effectively. Overall, SAPCG displayed a number of attractive properties that make it a promising candidate for future applications as an additive in detergent formulations