Purification and biochemical characterization of a novel thermostable serine alkaline protease from Aeribacillus pallidus C10: a potential additive for detergents

An extracellular thermostable alkaline serine protease enzyme from Aeribacillus pallidus C10 (GenBank No: KC333049), was purified 4.85 and 17. 32-fold with a yield of 26.9 and 19.56%, respectively, through DE52 anion exchange and Probond affinity chromatography. The molecular mass of the enzyme was determined through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with approximately 38.35 kDa. The enzyme exhibited optimum activity at pH 9 and at temperature 60 °C. It was determined that the enzyme had remained stable at the range of pH 7.0–10.0, and that it had preserved more than 80% of its activity at a broad temperature range (20–80 °C). The enzyme activity was found to retain more than 70% and 55% in the presence of organic solvents and commercial detergents, respectively. In addition, it was observed that the enzyme activity had increased in the presence of 5% SDS. KM and Vmax values were calculated as 0.197 mg/mL and 7.29 μmol.mL−1.min−1, respectively

A novel endo-beta-1,4-xylanase from Pediococcus acidilactici GC25; purification, characterization and application in clarification of fruit juices

GENC, BERNA/0000-0002-2790-9578; Adiguzel, Ahmet/0000-0001-8848-6647WOS: 000466621200059PubMed: 30753879A novel extracellular xylanase was purified and characterized from Pediococcus acidilactici GC25 (GenBank number: MF289522). the purification was 4.6-fold with a yield of 43.61% through acetone precipitation, Q-Sepharose, and CM-Sepharose ion change chromatography. the molecular weight of the enzyme was 48.15 kDa, and the optimum pH and temperature were 7.0 and 40 degrees C, respectively. the maximum activity was observed between 20 and 50 degrees C. Although it was active within a wide pH range (pH 2.0-9.0), it retained over 85% of its activity after 24 h incubation; and over 70% of its activity after 168 h incubation in neutral and alkaline pH. It was observed that the enzyme showed high stability with K+, Ba2+, Cd2+, Co2+, Sr2+, Mg2+, Ca2+, Al3+, Zn2+, and Ni2+ ions. the K-m and V-max for the xylanase were 3.10 mg mL(-1) and 4.66 U/mg protein, respectively. It was determined that treatment of different fruit juices with P. acidilactici GC25 xylanase improved the clarification. the highest increase in the reducing sugar amount and decrease in the turbidity was 24.47 +/- 1.08 and 21.22 +/- 0.58 for peach juice at 0.15 U/mL enzyme concentration. These results showed that the xylanase purified from P. acidilactici GC25 may have a wide potential in biotechnological processes of the food and baking industry. (C) 2019 Elsevier B.V. All rights reserved.Research Development Center of Ataturk UniversityAtaturk University [2015/54, FAD-2018-6352]; Ataturk University, TurkeyAtaturk UniversityThis research was conducted under the projects numbered 2015/54 and FAD-2018-6352 supported by the Research Development Center of Ataturk University. the authors acknowledged the support of Ataturk University, Turkey for this work