Detail
Článek
Web zdroj
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

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

R. Zhang, J. Zhou, Y. Gao, Y. Guan, J. Li, X. Tang, B. Xu, J. Ding, Z. Huang,

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

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc16013777

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.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc16013777
003      
CZ-PrNML
005      
20160506124058.0
007      
ta
008      
160506s2015 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1007/s12223-015-0391-1 $2 doi
024    7_
$a 10.1007/s12223-015-0391-1 $2 doi
035    __
$a (PubMed)25868895
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Zhang, Rui $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 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, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
245    10
$a Molecular and biochemical characterizations of a new low-temperature active mannanase / $c R. Zhang, J. Zhou, Y. Gao, Y. Guan, J. Li, X. Tang, B. Xu, J. Ding, Z. Huang,
520    9_
$a 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.
650    _2
$a sekvence aminokyselin $7 D000595
650    _2
$a bakteriální proteiny $x chemie $x genetika $x izolace a purifikace $x metabolismus $7 D001426
650    _2
$a nízká teplota $7 D003080
650    _2
$a stabilita enzymů $7 D004795
650    _2
$a kinetika $7 D007700
650    _2
$a molekulární sekvence - údaje $7 D008969
650    _2
$a konformace proteinů $7 D011487
650    _2
$a sekvenční seřazení $7 D016415
650    _2
$a Sphingobacterium $x chemie $x enzymologie $x genetika $7 D045249
650    _2
$a beta-mannosidasa $x chemie $x genetika $x izolace a purifikace $x metabolismus $7 D044902
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Zhou, Junpei $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 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, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Gao, Yajie $u College of Life Sciences, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Guan, Yaping $u College of Life Sciences, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Li, Junjun $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 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, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Tang, Xianghua $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 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, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Xu, Bo $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 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, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Ding, Junmei $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 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, Kunming, 650500, People's Republic of China. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China.
700    1_
$a Huang, Zunxi $u Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. huangzunxi@163.com. College of Life Sciences, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. huangzunxi@163.com. Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Kunming, 650500, People's Republic of China. huangzunxi@163.com. Key Laboratory of Enzyme Engineering, Yunnan Normal University, No. 1 Yuhua District, Chenggong, Kunming, Yunnan, 650500, People's Republic of China. huangzunxi@163.com.
773    0_
$w MED00011005 $t Folia microbiologica $x 1874-9356 $g Roč. 60, č. 6 (2015), s. 483-92
856    41
$u https://pubmed.ncbi.nlm.nih.gov/25868895 $y Pubmed
910    __
$a ABA008 $b online $c sign $y a $z 0
990    __
$a 20160506 $b ABA008
991    __
$a 20160506124159 $b ABA008
999    __
$a ok $b bmc $g 1123871 $s 938189
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2015 $b 60 $c 6 $d 483-92 $e 20150414 $i 1874-9356 $m Folia microbiologica $n Folia microbiol. (Prague) $x MED00011005
LZP    __
$a Pubmed-20160506

Najít záznam

Citační ukazatele

Možnosti archivace