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Purification and partial characterization of polygalacturonase from Streptomyces lydicus
- Source :
-
Bioresource Technology . Sep2008, Vol. 99 Issue 14, p6697-6701. 5p. - Publication Year :
- 2008
-
Abstract
- Polygalacturonase produced by Streptomyces lydicus was purified to homogeneity by ultrafiltration and a combination of ion exchange and gel filtration chromatographic procedures. The purified enzyme was an exo-polygalacturonase with a molecular weight of 43kDa. It was optimally active at 50°C and pH 6.0. The enzyme was stable from pH 4.0 to 7.0 and at or below 45°C for 90min. K m value for polygalacturonic acid was 1.63mg/mL and the corresponding V max was 677.8μM min−1 mg−1. The inhibition constant (K i) for gluconic acid d-lactone was 20.75mM. Purified enzyme had been inhibited by N-bromosuccinimide, while l-tryptophan could induce enzyme activity, indicating the involvement of tryptophan at the active site. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 09608524
- Volume :
- 99
- Issue :
- 14
- Database :
- Academic Search Index
- Journal :
- Bioresource Technology
- Publication Type :
- Academic Journal
- Accession number :
- 32477010
- Full Text :
- https://doi.org/10.1016/j.biortech.2007.10.002