共 43 条
Characterization of a New Cold-Adapted and Salt-Activated Polysaccharide Lyase Family 7 Alginate Lyase from Pseudoalteromonas sp SM0524
被引:67
作者:
Chen, Xiu-Lan
[1
,2
]
Dong, Sheng
[1
,2
]
Xu, Fei
[1
,2
]
Dong, Fang
[1
,2
]
Li, Ping-Yi
[1
,2
,3
]
Zhang, Xi-Ying
[1
,2
]
Zhou, Bai-Cheng
[2
]
Zhang, Yu-Zhong
[1
,2
,3
,4
]
Xie, Bin-Bin
[1
,2
]
机构:
[1] Shandong Univ, State Key Lab Microbial Technol, Jinan, Peoples R China
[2] Shandong Univ, Marine Biotechnol Res Ctr, Jinan, Peoples R China
[3] Shandong Univ, Inst Marine Sci & Technol, Jinan, Peoples R China
[4] Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China
基金:
美国国家科学基金会;
关键词:
marine bacteria;
alginate lyase;
cold-adapted enzyme;
salt-activated;
polysaccharide lyase family 7;
PSYCHROPHILIC ENZYMES;
MAJOR SOURCES;
CLONING;
SEA;
AGARIVORANS;
VIBRIO;
GENES;
PURIFICATION;
BACTERIA;
D O I:
10.3389/fmicb.2016.01120
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
Marine bacterial alginate lyases play a role in marine alginate degradation and carbon cycling. Although a large number of alginate lyases have been characterized, reports on alginate lyases with special characteristics are still rather less. Here, a gene alyPM encoding an alginate lyase of polysaccharide lyase family 7 (PL7) was cloned from marine Pseudoalteromonas sp. SM0524 and expressed in Escherichia coil. AIyPM shows 41% sequence identity to characterized alginate lyases, indicating that AIyPM is a new PL7 enzyme. The optimal pH for AIyPM activity was 8.5. AIyPM showed the highest activity at 30 degrees C and remained 19% of the highest activity at 5 degrees C. AIyPM was unstable at temperatures above 30 degrees C and had a low T-m of 37 degrees C. These data indicate that AIyPM is a cold-adapted enzyme. Moreover, AIyPM is a salt-activated enzyme. AIyPM activity in 0.5-1.2 M NaCI was sixfolds higher than that in 0 M NaCI, probably caused by a significant increase in substrate affinity, because the Km of AIyPM in 0.5 M NaCI decreased more than 20-folds than that in 0 M NaCI. AIyPM preferably degraded polymannuronate and mainly released dimers and trimers. These data indicate that AIyPM is a new PL7 endo-alginate lyase with special characteristics.
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页数:9
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