Journal of Microbiology

Identification of Petriella setifera LH and Characterization of Its Crude Carboxymethyl Cellulase for Application in Denim Biostoning: Xi-Hua Zhao , Wei Wang , Dong-Zhi Wei; J. Microbiol. 2013;51(1):82-87. Published online March 2, 2013; DOI: https://doi.org/10.1007/s12275-013-2370-z

Abstract: The phylogenetic tree of the partial elongation factor-1 alpha gene fits better than the partial 18S rDNA for generic classification. From the results of the molecular tree and analysis of morphological characters, Petriella setifera LH was identified. It can be induced to produce carboxymethyl cellulase (CMCase). The crude CMCase only shows a 44.1-kDa band by activity staining after SDS-PAGE. It is optimally active at 55°C and pH 6.0, and is stable from pH 5.0–8.0 and at 45°C or below. The crude CMCase, which is not affected by Co2+, is strongly activated in the presence of 10 mM Na+, K+, Ca2+, Mg2+, EDTA, and Mn2+. It is strongly inhibited by 10 mM Fe2+, Pb2+, Al3+, Zn2+, Ag+, Fe3+, and Cu2+. When compared with denim treatment by Novoprime A800 (a commercial neutral cellulase), crude CMCase exhibits a similar fabric weight loss and indigo dye removal. These results indicate that crude CMCase has potential application in denim biostoning.

Molecular Cloning, Purification, and Characterization of a Novel, Acidic, pH-Stable Endoglucanase from Martelella mediterranea: Junli Dong , Yuzhi Hong , Zongze Shao , Ziduo Liu; J. Microbiol. 2010;48(3):393-398. Published online June 23, 2010; DOI: https://doi.org/10.1007/s12275-010-9361-0

Abstract: A novel gene encoding an endoglucanase designated Cel5D was cloned from a marine bacterium Martelella mediterranea by genomic library. The gene had a 1,113 bp opening reading frame encoding a 371-amino-acid protein with a molecular mass of 40,508 Da and containing a putative signal peptide (41 amino acids). Cel5D had low similarity (48-51% identity) with other known endoglucanases and consisted of one single catalytic domain, which belonged to the glycosyl hydrolase family 5. The maximum activity of Cel5D was observed at 60°C and pH 5.0. Cel5D displayed broad pH stability within the range of pH 3.0-11.0 and retained hydrolytic activity in the presence of a wide variety of metal ions and some chemical reagents. These characteristics suggest that the enzyme has considerable potential in industrial applications.

Purification of carbosymethyl cellulase from hybrid between aspergillus niger and penicillium verruculosum: Yang, Young Ki , Lee, Jung Sup , Park, Hyung Nam , Moon, Myung Nim , Kim, Hong Sub , Kim, Jong Se , Lim, Chae Young , Rhee, Young Ha; J. Microbiol. 1996;34(1):90-94.

Abstract: The carboxymethyl cellulase (CMCase) was purified from the induced culture filtrate of hybrid TAPW15703 between Aspergillus niger and penicillium verruculosum made by nuclear transfer. The enzyme was purified 80 fold with an overall yield 17% from the culture medium by ammonium sulfate fractionation, Sephadex G-75 gel permeation chromatography, and DEAE-ion exchange column chromatography. The molecular weight of the CMCase has estimated to be 32,000 daltons on SDS-polyacrylamide gel electrophoresis and Sephadex G-150 gel permeation chromatography. The purified enzyme functions optimally at pH 4.0 and 40℃. The Km value for carbosymethyl cellulose was 68 mM. The enzyme activity was increased by the presence of Mg^2+ and Mn^2+.

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