Zinc biosorption and bioaccumulation by a novel extremely Zn tolerant Streptomyces K11 strain isolated from highly alkaline environment were examined. Temperature, similarly as biosorbent preparation, has negligible effect on the biosorption capacity but very strong effect on the process kinetics. Initial adsorption rate increased almost 10 times with the temperature increase from 10 to 50 °C and it was 30 times higher when non-dried biomass was used. The biosorption study revealed that the process was mainly chemically controlled, however at lower temperature intra-particle diffusion played significant role in the zinc biosorption. The experimental data fitted the Langmuir isotherm model with the maximum biosorption capacity 0.75 mmol g. The results of bioaccumulation onto a living biomass of Streptomyces K11 indicated very high bioaccumulation capacity of 4.4 mmol g. Zinc extracellular uptake (43%) slightly exceeded the intracellular accumulation (36%). High zinc bioaccumulation capacity was obviously related to extremely high zinc tolerance of Streptomyces K11.
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http://dx.doi.org/10.1016/j.ecoenv.2018.09.123 | DOI Listing |
Ecotoxicol Environ Saf
January 2019
Department of Microbiology, Institute of Biology and Ecology, Faculty of Science, Pavol Jozef Safarik University, Srobarova 2, 04154 Kosice, Slovakia; Institute of Animal Physiology, Slovak Academy of Sciences, Soltesovej 4-6, 04001 Kosice, Slovakia.
Int J Syst Evol Microbiol
May 2018
Kitasato Institute for Life Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan.
Actinomycete strain K11-0400 was isolated from a soil sample collected in the Ogasawara Islands (also known as the Bonin Islands), Tokyo, Japan. Mature spore chains of strain K11-0400 had more than 20 spores per chain. The strain contained ll-diaminopimelic acid as the diamino acid in whole-cell hydrolysates, and MK-9(H6) and MK-9(H4) were the predominant menaquinones.
View Article and Find Full Text PDFBiotechnol Lett
May 2013
State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China.
The keratinase Sfp2, produced by Streptomyces fradiae var. k11, is a serine alkaline protease first synthesized as pre-pro-mature precursor, of which the N-terminal propeptide must be autocatalytically cleaved on the C-terminal of P1 amino acid to produce mature enzyme. Single amino acid substitutions were introduced at positions -1 and -2 to improve the expression level of mature Sfp2.
View Article and Find Full Text PDFAppl Biochem Biotechnol
March 2010
Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing 100081, People's Republic of China.
An aminopeptidase gene fragment was isolated from a keratin-degrading strain, Streptomyces fradiae var. k11, by PCR amplification using a degenerate primer set designed based on the partial amino acid sequence of the native enzyme. The gene, designated sfap, encoded a polypeptide of 461 amino acids comprised of three domains: a signal peptide, a mature region, and a C-terminal propeptide.
View Article and Find Full Text PDFJ Microbiol Biotechnol
March 2008
Microbial Engineering Department, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
The gene SfXyn10, which encodes a protease-resistant xylanase, was isolated using colony PCR screening from a genomic library of a feather-degrading bacterial strain Streptomyces fradiae var. k11. The full-length gene consists of 1,437 bp and encodes 479 amino acids, which includes 41 residues of a putative signal peptide at its N terminus.
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