Hydroperoxide Lyase and Leaf Aldehyde Formation can be Greatly Increased in Leaves

2003 ◽  
pp. 299-302 ◽  
Author(s):  
Wipawan Siangdung ◽  
Hirotada Fukushige ◽  
David Hildebrand
Keyword(s):  
Hydroperoxide Lyase ◽  
Leaf Aldehyde

scholarly journals Optimizing the Production of Recombinant Hydroperoxide Lyase in Escherichia coli Using Statistical Design

Catalysts ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 176
Author(s):  
Sophie Vincenti ◽  
Magali Mariani ◽  
Jessica Croce ◽  
Eva Faillace ◽  
Virginie Brunini-Bronzini de Caraffa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Expression System ◽  
Scale Up ◽  
Food Additives ◽  
Statistical Design ◽  
Green Leaf Volatiles ◽  
Hydroperoxide Lyase ◽  
Soluble Enzyme ◽  
Leaf Volatiles ◽  
Conversion Rates

Hydroperoxide lyase (HPL) catalyzes the synthesis of volatiles C6 or C9 aldehydes from fatty acid hydroperoxides. These short carbon chain aldehydes, known as green leaf volatiles (GLV), are widely used in cosmetic industries and as food additives because of their “fresh green” aroma. To meet the growing demand for natural GLVs, the use of recombinant HPL as a biocatalyst in enzyme-catalyzed processes appears to be an interesting application. Previously, we cloned and expressed a 13-HPL from olive fruit in Escherichia coli and showed high conversion rates (up to 94%) during the synthesis of C6 aldehydes. To consider a scale-up of this process, optimization of the recombinant enzyme production is necessary. In this study, four host-vector combinations were tested. Experimental design and response surface methodology (RSM) were used to optimize the expression conditions. Three factors were considered, i.e., temperature, inducer concentration and induction duration. The Box–Behnken design consisted of 45 assays for each expression system performed in deep-well microplates. The regression models were built and fitted well to the experimental data (R2 coefficient > 97%). The best response (production level of the soluble enzyme) was obtained with E. coli BL21 DE3 cells. Using the optimal conditions, 2277 U L−1of culture of the soluble enzyme was produced in microliter plates and 21,920 U L−1of culture in an Erlenmeyer flask, which represents a 79-fold increase compared to the production levels previously reported.

scholarly journals The rice hydroperoxide lyase OsHPL3 functions in defense responses by modulating the oxylipin pathway

2012 ◽  
Vol 71 (5) ◽  
pp. 763-775 ◽  
Author(s):  
Xiaohong Tong ◽  
Jinfeng Qi ◽  
Xudong Zhu ◽  
Bizeng Mao ◽  
Longjun Zeng ◽  
...  
Keyword(s):  
Defense Responses ◽  
Hydroperoxide Lyase

Production of flavor compounds by hydroperoxide lyase from enzymatic extracts of Penicillium sp.

2002 ◽  
Vol 19-20 ◽  
pp. 479-487 ◽  
Author(s):  
Selim Kermasha ◽  
Xavier Perraud ◽  
Barbara Bisakowski ◽  
Florence Husson
Keyword(s):  
Hydroperoxide Lyase ◽  
Flavor Compounds ◽  
Penicillium Sp

Lipoxygenase and hydroperoxide lyase activities in ripening tomato fruit

1996 ◽  
Vol 7 (1-2) ◽  
pp. 97-107 ◽  
Author(s):  
John C.M. Riley ◽  
Claude Willemot ◽  
John E. Thompson
Keyword(s):  
Tomato Fruit ◽  
Hydroperoxide Lyase

“Biosynthesis of volatile compounds by hydroperoxide lyase enzymatic activity during virgin olive oil extraction process”

2018 ◽  
Vol 111 ◽  
pp. 220-228 ◽  
Author(s):  
Araceli Sánchez-Ortiz ◽  
Mohamed Aymen Bejaoui ◽  
Angélica Quintero-Flores ◽  
Antonio Jiménez ◽  
Gabriel Beltrán
Keyword(s):  
Enzymatic Activity ◽  
Olive Oil ◽  
Volatile Compounds ◽  
Virgin Olive Oil ◽  
Extraction Process ◽  
Oil Extraction ◽  
Hydroperoxide Lyase
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