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Autor: Li, Junjun

3 záznamů v BMČ Filtry

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A novel surfactant-, NaCl-, and protease-tolerant β-mannanase from Bacillus sp. HJ14

Zhang, Rui
Autor Zhang, Rui Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Song, Zhifeng
Autor Song, Zhifeng College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China
Wu, Qian
Autor Wu, Qian Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Zhou, Junpei
Autor Zhou, Junpei Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Li, Junjun
Autor Li, Junjun Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Mu, Yuelin
Autor Mu, Yuelin Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Tang, Xianghua
Autor Tang, Xianghua Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Xu, Bo
Autor Xu, Bo Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Ding, Junmei
Autor Ding, Junmei Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China
Deng, Shucan
Autor Deng, Shucan College of Life Sciences, Yunnan Normal University, No.1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China

Folia microbiologica. 2016 ; 61 (3) : 233-42. [pub] 20151021

Folia microbiol. (Prague)
ISSN 1874-9356
Medvik
Zdroj

A glycoside hydrolase family 5 β-mannanase-encoding gene was cloned from Bacillus sp. HJ14 isolated from saline soil in Heijing town. Coding sequence of mature protein (without the predicted signal peptide from M1 to A30) was successfully expressed in Escherichia coli BL21 (DE3). Purified recombinant mannanase (rMan5HJ14) exhibited optimal activity at pH 6.5 and 65 °C. The enzyme showed good salt tolerance, retaining more than 56 % β-mannanase activity at 3.0-30.0 % (w/v) NaCl and more than 94 % of the initial activity after incubation with 3.0-30.0 % (w/v) NaCl at 37 °C for 60 min. Almost no mannanase activity was lost after incubation of rMan5HJ14 with trypsin, proteinase K, and Alcalase at 37 °C for 60 min. Surfactants and chelating agents, namely SDS, CTAB, Tween 80, Triton X-100, EDTA, and sodium tripolyphosphate, showed little or no effect (retaining >82.4 % activity) on enzymatic activity. Liquid detergents, namely Tupperware, Walch, Bluemoon, Tide, and OMO, also showed little or no effect (retaining >72.4 % activity) on enzymatic activity at 0.5-2.0 % (v/v). The enzyme further presents a high proportion (11.97 %) of acidic amino acid residues (D and E), which may affect the SDS and NaCl tolerance of the enzyme. Together, the mannanase may be an alternative for potential use in liquid detergent industry.

Web zdroj

Molecular and biochemical characterizations of a new low-temperature active mannanase

Folia microbiologica. 2015 ; 60 (6) : 483-92. [pub] 20150414

Folia microbiol. (Prague)
ISSN 1874-9356
Medvik
Zdroj

A mannanase-coding gene was cloned from Sphingobacterium sp. GN25 isolated from the feces of Grus nigricollis. The gene encodes a 371-residue polypeptide (ManAGN25) showing less than 74 % identity with a number of hypothetical proteins and putative glucanases and mannanases. Before experiment's performance, ManAGN25 was predicted to be a low-temperature active mannanase based on the molecular characterization, including (1) ManAGN25 shared the highest identity of 41.1 % with the experimentally verified low-temperature active mannanase (ManAJB13) from Sphingomonas sp. JB13; (2) compared with their mesophilic and thermophilic counterparts, ManAGN25 and ManAJB13 had increased number of amino acid residues around their catalytic sites; (3) these increased number of amino acid residues built longer loops, more α-helices, and larger total accessible surface area and packing volume. Then the experiments of biochemical characterization verified that the purified recombinant ManAGN25 is a low-temperature active mannanase: the enzyme showed apparently optimal activity at 35-40 °C and retained 78.2, 44.8, and 15.0 % of its maximum activity when assayed at 30, 20, and 10 °C, respectively; the half-life of the enzyme was approximately 60 min at 37 °C; the enzyme presented a K m of 4.2 mg/ml and a k cat of 0.4/s in McIlvaine buffer (pH 7.0) at 35 °C using locust bean gum as the substrate; and the activation energy for hydrolysis of locust bean gum by the enzyme was 36.0 kJ/mol. This study is the first to report the molecular and biochemical characterizations of a mannanase from a strain.

Web zdroj

A thermo-halo-tolerant and proteinase-resistant endoxylanase from Bacillus sp. HJ14

Folia microbiologica. 2014 ; 59 (5) : 423-31.

Folia microbiol. (Prague)
ISSN 1874-9356
Medvik
Zdroj

A glycosyl hydrolase family 10 endoxylanase from Bacillus sp. HJ14 was grouped in a separated cluster with another six Bacillus endoxylanases which have not been characterized. These Bacillus endoxylanases showed less than 52% amino acid sequence identity with other endoxylanases and far distance with endoxylanases from most microorganisms. Signal peptide was not detected in the endoxylanase. The endoxylanase was expressed in Escherichia coli BL21 (DE3), and the purified recombinant enzyme (rXynAHJ14) was characterized. rXynAHJ14 was apparent optimal at 62.5 °C and pH 6.5 and retained more than 55% of the maximum activity when assayed at 40-75 °C, 23% at 20 °C, 16% at 85 °C, and even 8% at 0 °C. Half-lives of the enzyme were more than 60 min, approximately 25 and 4 min at 70, 75, and 80 °C, respectively. The enzyme exhibited more than 62% xylanase activity and stability at the concentration of 3-30% (w/v) NaCl. No xylanase activity was lost after incubation of the purified rXynAHJ14 with trypsin and proteinase K at 37 °C for 60 min. Different components of oligosaccharides were detected in the time-course hydrolysis of beechwood xylan by the enzyme. During the simulated intestinal digestion phase in vitro, 11.5-19.0, 15.3-19.0, 21.9-27.7, and 28.2-31.2 μmol/mL reducing sugar were released by the purified rXynAHJ14 from soybean meal, wheat bran, beechwood xylan, and rapeseed meal, respectively. The endoxylanase might be an alternative for potential applications in the processing of sea food and saline food and in aquaculture as agastric fish feed additive.

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