125103-95-9Relevant academic research and scientific papers
Process Optimisation Studies and Aminonitrile Substrate Evaluation of Rhodococcus erythropolis SET1, A Nitrile Hydrolyzing Bacterium
Coady, Tracey M.,Coffey, Lee,Kinsella, Michael,Lennon, Claire M.,Mareya, Tatenda M.,O'Reilly, Catherine
, p. 512 - 520 (2020/10/02)
A comprehensive series of optimization studies including pH, solvent and temperature were completed on the nitrile hydrolyzing Rhodococcus erythropolis bacterium SET1 with the substrate 3-hydroxybutyronitrile. These identified temperature of 25 °C and pH of 7 as the best conditions to retain enantioselectivity and activity. The effect of the addition of organic solvents to the biotransformation mixture was also determined. The results of the study suggested that SET1 is suitable for use in selected organo-aqueous media at specific ratios only. The functional group tolerance of the isolate with unprotected and protected β-aminonitriles, structural analogues of β-hydroxynitriles was also investigated with disappointingly poor isolated yields and selectivity obtained. The isolate was further evaluated with the α- aminonitrile phenylglycinonitrile generating acid in excellent yield and ee (>99 % (S) – isomer and 50 % yield). A series of pH studies with this substrate indicated pH 7 to be the optimum pH to avoid product and substrate degradation.
A high throughput screening strategy for the assessment of nitrile-hydrolyzing activity towards the production of enantiopure β-hydroxy acids
Coady, Tracey M.,Coffey, Lee V.,O'Reilly, Catherine,Owens, Erica B.,Lennon, Claire M.
, p. 150 - 155 (2013/10/01)
Nitrile hydrolysing enzymes have found wide use in the pharmaceutical industry for the production of fine chemicals. This work presents a strategy that facilitates the rapid identification of bacterial isolates demonstrating nitrile hydrolysing activity. The strategy incorporates toxicity, starvation and induction studies along with subsequent colorimetric screening for activity, further focusing the assessment towards the substrates of interest. This high-throughput strategy uses a 96 well plate system, and has enabled the rapid biocatalytic screening of 256 novel bacterial isolates towards β-hydroxynitriles. Results demonstrate the strategy's potential to rapidly assess a variety of β-hydroxynitriles including aliphatic, aromatic and dinitriles. A whole cell catalyst Rhodococcus erythropolis SET1 was identified and found to catalyse the hydrolysis of 3-hydroxybutyronitrile with remarkably high enantioselectivity under mild conditions, to afford (S)-3-hydroxybutyric acid in 42% yield and >99.9% ee. The biocatalytic capability of this strain including the variation of parameters such as temperature and time were further investigated and all results indicate the presence of a highly enantioselective if not enantiospecific nitrilase enzyme within the microbial whole cell.
Thiacrown Ether Technology in Lipase-Catalyzed Reaction: Scope and Limitation for Preparing Optically Active 3-Hydroxyalkanenitriles and Application to Insect Pheromone Synthesis
Itoh, Toshiyuki,Mitsukura, Koichi,Kanphai, Wipa,Takagi, Yumiko,Kihara, Hiroshi,Tsukube, Hiroshi
, p. 9165 - 9172 (2007/10/03)
Both reaction rate and enantioselectivity in Pseudomonas cepacia lipase (PCL)-catalyzed hydrolysis of 3-hydroxyalkanenitrile acetates were significantly changed by the addition of catalytic amounts of thiacrown ether (1,4,8,11-tetrathiacyclotetradecane). Although the reaction rate of various nitriles was accelerated, the enantioselectivity greatly depended on the nature of the substrate. Among 10 substrates tested, thiacrown ether offered highest enantioselectivity in PCL-catalyzed hydrolysis of 1-(cyanomehtyl)propyl acetate. Forty or more times this crown ether, molarity based on the enzyme, was required to attain an acceptably high reaction rate and enantioselectivity. Applying this technology, we succeeded in synthesizing the optically pure attractant pheromone of ant Myrmica scabrinodis (A), (R)-3-octanol and its antipode of (S)-isomer in good overall yields.
Crown ethers as regulators of enzymatic reactions: Enhanced reaction rate and enantioselectivity in lipase-catalyzed hydrolysis of 2-cyano-1-methylethyl acetate
Itoh, Toshiyuki,Takagi, Yumiko,Murakami, Takako,Hiyama, Yuji,Tsukube, Hiroshi
, p. 2158 - 2163 (2007/10/03)
Both reaction rate and enantioselectivity in lipase-catalyzed hydrolysis of 2-cyano-1-methylethyl acetate were significantly changed by addition of some crown ethers. Although various crown ethers accelerated the reaction rate, the enantioselectivity greatly depended on the nature of each one. Among 27 crown ethers and 5 polyethers tested, benzo-crown, armed azacrown, and thiacrown ethers offered high enantioselectivity of the lipase-catalyzed hydrolysis. Hydrophobicity and chirality of the crown ether did not affect the hydrolysis behavior, but its concentration greatly influenced enantioselectivity. Two hundred fifty or more times the crown ether, molarity based on the enzyme, was required to attain satisfactorily high reaction rate and enantioselectivity.
Enhanced reaction rate and enantioselectivity in lipase-catalyzed hydrolysis by addition of a crown ether
Itoh,Hiyama,Betchaku,Tsukube
, p. 2617 - 2620 (2007/10/02)
Both reaction rate and enantioselectivity in a lipase-catalyzed hydrolysis of β-acetoxybutyronitrile were significantly enhanced by addition of hydroxymethyl-12-crown-4.
Enhanced Enantioselectivity of the Lipase-catalyzed Hydrolysis by the Addition of a Catalytic Amount of an Amino Alcohol
Itoh, Toshiyuki,Ohira, Eri,Takagi, Yumiko,Nishiyama, Shigenori,Nakamura, Kaoru
, p. 624 - 627 (2007/10/02)
L-Methioninol (L-MetOH) was discovered to be an effective additive for improving the enantioselectivity of lipase-catalyzed hydrolysis.It was found that L-MetOH accelerated the enzyme-catalyzed hydrolysis of (R)-3-acetoxybutyronitrile (1) and inhibited that of (S)-1.
Enhanced Enantioselectivity of an Enzymatic Reaction by the Sulfur Functional Group. A Simple Preparation of Optically Active β-Hydroxy Nitriles Using a Lipase
Itoh, Toshiyuki,Takagi, Yumiko,Nishiyama, Shigenori
, p. 1521 - 1524 (2007/10/02)
The enantioselectivity of a lipase-catalyzed hydrolysis was improved by varying the acyl residue into the sulfur functional one, i.e. the β-(phenylthio)- or β-(methylthio)acetoxy group, from acetate or valerate to realize satisfactory resolution of β-hydr
Stereorecognition Enhancement by the Sulfur Functional Group in the Lipase Hydrolysis. An Efficient Synthesis of the Optically Active β-Hydroxy Nitriles
Itoh, Toshiyuki,Takagi, Yumiko
, p. 1505 - 1506 (2007/10/02)
β-phenylthio and β-methylthioacetoxy nitriles have been found to be good substrates for the kinetic resolution by lipase to give optically active β-hydroxy nitriles with high enantioselectivity.
