2012
DOI: 10.1016/j.molcatb.2012.04.015
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Characterization of a novel esterase isolated from intertidal flat metagenome and its tertiary alcohols synthesis

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Cited by 24 publications
(16 citation statements)
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“…Biochemical properties, in particular pH and temperature range and stability, determine the conditions under which a specific industrial process must operate [1]. The optimal pH of RmEstB is 7.5, which is similar to that of most other reported esterases [18,35,43], higher than that of a HSL esterase from Pyrobaculum calidifontis [4] and RmEstA from R. miehei [29], and lower than that of a HSL esterase from a soil DNA library [42] and EstK from P. mandelii [39]. Most microbial esterases exhibit narrow pH stabilities under alkaline conditions [11,38,44].…”
Section: Discussionmentioning
confidence: 53%
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“…Biochemical properties, in particular pH and temperature range and stability, determine the conditions under which a specific industrial process must operate [1]. The optimal pH of RmEstB is 7.5, which is similar to that of most other reported esterases [18,35,43], higher than that of a HSL esterase from Pyrobaculum calidifontis [4] and RmEstA from R. miehei [29], and lower than that of a HSL esterase from a soil DNA library [42] and EstK from P. mandelii [39]. Most microbial esterases exhibit narrow pH stabilities under alkaline conditions [11,38,44].…”
Section: Discussionmentioning
confidence: 53%
“…It is interesting that RmEstB efficiently hydrolyzed the tertiary alcohol ester linalyl acetate to yield linalyl alcohol, similar to two esterases from metagenomic DNA libraries [42,43], while most other esterases and lipases do not possess this ability [43]. Moreover, the conversion yield (98%) is much higher than those of the other two esterases with a conversion yield of less than 50% [42,43]. This property makes this enzyme attractive for possible practical application in the production of flavor compounds in the food industry.…”
Section: Discussionmentioning
confidence: 99%
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“…Six of them (Lip5.1_5, Lip5.3_3, Lip5.5_4, Lip5.13_3, Lip5.14_3, and Lip5.19_3) have been assigned to family IV. This esterase family appears to be highly represented in marine metagenomes, as out of 34 esterases identified in 8 screens of marine metagenomes, 27 have been classified as family IV esterases (39,(45)(46)(47)(48)(49)(50)(51). We have assigned one of the esterase loci identified here (Lip5.13_1) to esterase family V, which appears to count relatively few members.…”
Section: Discussionmentioning
confidence: 74%