Enzymatic resolution of racemic sulcatol by lipase from Candida Antarctica in a large scale

2010 ◽  
Vol 7 (4) ◽  
pp. 883-889 ◽  
Author(s):  
H. V. Ferreira ◽  
L. C. Rocha ◽  
R. P. Severino ◽  
R. B. Viana ◽  
A. B. F. da Silva ◽  
...  
Keyword(s):  
Large Scale ◽  
Candida Antarctica ◽  
Enzymatic Resolution

scholarly journals Electrophoretic and zymographic techniques for production monitoring of two lipase forms from Candida antarctica DSM 70725

2012 ◽  
Vol 66 (2) ◽  
pp. 201-206
Author(s):  
Aleksandra Dimitrijevic ◽  
Dusan Velickovic ◽  
Ratko Jankov ◽  
Nenad Milosavic
Keyword(s):  
Molecular Weight ◽  
Large Scale ◽  
Fermentation Broth ◽  
Candida Antarctica ◽  
Simple Method ◽  
Wide Range ◽  
Work Production ◽  
Lipase A ◽  
Dimeric Form ◽  
Hydrolysis Of

Yeast Candida antarctica produces two lipase forms, which are widely used as catalysts in variety of organic reactions, many of which are applied on a large scale. In this work, production of two forms of lipase from C. antarctica DSM 70725 (CAL A and CAL B) was monitored during seven days of cultivation in the optimal medium using different electrophoretic and zymographic techniques. According to electrophoresis after silver staining, C. antarctica lipase A (molecular mass 45 kDa) was produced starting from the second day of cultivation. C. antarctica lipase B (CAL B) was also produced starting from the second day, but protein was present in the fermentation broth predominantly as dimer (molecular weight 66 kDa), while presence of monomeric form of CAL B (molecular weight of 33 kDa) was observed starting from the fourth day of cultivation. Both types of zymograms (based on hydrolysis and synthesis reactions) were used for detection of lipase activity in the fermentation broth. C. antarctica lipase A showed activity only in hydrolytic zymogram, when ?-naphtyl butyrate was used as substrate. In the same zymogram, with ?-naphtyl acetate as substrate no CAL A activity was detected. Similarly, CAL A showed no activity in synthesis based zymograms towards oleic acid and octanol as substrates, indicating that CAL A is not active towards very short or long-chain substrates. As opposite of CAL A, both monomeric and dimeric form of CAL B were detected in the all zymograms, suggesting that CAL B is active towards wide range of substrates, regardless to the chain length. Thus, zymogram based on hydrolysis of ?-naphtyl butyrate represents a simple method for monitoring the production of two forms of lipase from C. antarctica, that greatly differ in their characteristics.

Enzymatic resolution of methyl N-alkyl-azetidine-2-carboxylates by Candida antarctica lipase-mediated ammoniolysis

1998 ◽  
Vol 9 (3) ◽  
pp. 429-435 ◽  
Author(s):  
Wim A.J Starmans ◽  
Roy G Doppen ◽  
Lambertus Thijs ◽  
Binne Zwanenburg
Keyword(s):  
Candida Antarctica ◽  
Candida Antarctica Lipase ◽  
Enzymatic Resolution

Highly enantioselective enzymatic resolution of cis-fused octalols mediated by Candida antarctica lipase (Novozym 435)

2006 ◽  
Vol 17 (13) ◽  
pp. 1990-1994 ◽  
Author(s):  
Tiago O. Vieira ◽  
Helena M.C. Ferraz ◽  
Leandro H. Andrade ◽  
André L.M. Porto
Keyword(s):  
Candida Antarctica ◽  
Novozym 435 ◽  
Candida Antarctica Lipase ◽  
Enzymatic Resolution

Enantiomerically Pure Organoseleno-1-arylethanols (III) and (IX) by Enzymatic Resolution with Candida antarctica Lipase: Novozym 435.

ChemInform ◽  
2007 ◽  
Vol 38 (43) ◽  
Author(s):  
Alvaro T. Omori ◽  
Leonardo F. Assis ◽  
Leandro H. Andrade ◽  
Joao V. Comasseto ◽  
Andre L. M. Porto
Keyword(s):  
Candida Antarctica ◽  
Novozym 435 ◽  
Candida Antarctica Lipase ◽  
Enzymatic Resolution ◽  
Enantiomerically Pure

Biotransformations of Mannich bases and propiophenones by Brazilian microorganisms and enzymatic resolution of phenylpropanols by lipase from Candida antarctica (Novozym 435)

2007 ◽  
Vol 40 (2) ◽  
pp. 362-369 ◽  
Author(s):  
Cristiano Raminelli ◽  
Edna Kagohara ◽  
Vivian H. Pellizari ◽  
João V. Comasseto ◽  
Leandro H. Andrade ◽  
...  
Keyword(s):  
Mannich Bases ◽  
Candida Antarctica ◽  
Novozym 435 ◽  
Enzymatic Resolution

Enzymatic Resolution of β-Amino Methyl Esters using Lipase B from Candida antarctica.

2008 ◽  
Author(s):  
Jaime Escalante ◽  
Enrique Díaz-Herrera ◽  
Eusebio Juaristi
Keyword(s):  
Methyl Esters ◽  
Candida Antarctica ◽  
Lipase B ◽  
Enzymatic Resolution

Enzymatic resolution of racemic secondary alcohols by lipase B from Candida antarctica

2000 ◽  
Vol 77 (10) ◽  
pp. 1015-1019 ◽  
Author(s):  
Ramesh N. Patel ◽  
Amit Banerjee ◽  
Venkata Nanduri ◽  
Animesh Goswami ◽  
F. T. Comezoglu
Keyword(s):  
Candida Antarctica ◽  
Secondary Alcohols ◽  
Lipase B ◽  
Enzymatic Resolution

Enantiomerically pure organoseleno-1-arylethanols by enzymatic resolution with Candida antarctica lipase: Novozym 435

2007 ◽  
Vol 18 (9) ◽  
pp. 1048-1053 ◽  
Author(s):  
Álvaro T. Omori ◽  
Leonardo F. Assis ◽  
Leandro H. Andrade ◽  
João V. Comasseto ◽  
André L.M. Porto
Keyword(s):  
Candida Antarctica ◽  
Novozym 435 ◽  
Candida Antarctica Lipase ◽  
Enzymatic Resolution ◽  
Enantiomerically Pure

Enzymatic resolution of N-protected-β3-amino methyl esters, using lipase B from Candida antarctica

2005 ◽  
Vol 16 (3) ◽  
pp. 629-634 ◽  
Author(s):  
Patricia Flores-Sánchez ◽  
Jaime Escalante ◽  
Edmundo Castillo
Keyword(s):  
Methyl Esters ◽  
Candida Antarctica ◽  
Lipase B ◽  
Enzymatic Resolution

A two-step enzymatic resolution process for large-scale production of (S)- and (R)-ethyl-3-hydroxybutyrate

2001 ◽  
Vol 74 (3) ◽  
pp. 256-263 ◽  
Author(s):  
Ayelet Fishman ◽  
Michael Eroshov ◽  
Shani Sheffer Dee-Noor ◽  
Jan van Mil ◽  
Uri Cogan ◽  
...  
Keyword(s):  
Large Scale ◽  
Scale Production ◽  
Enzymatic Resolution ◽  
Resolution Process ◽  
Large Scale Production
Sign in / Sign up

Export Citation Format

Share Document