Thermomyces lanuginosus

Several other processes were investigated and developed as well, e.g., a) Am-bruticin S production in airlift and stirred tank reactor b) high-cell density cultivation of E. coli and production of rDNA products c) production of thermostable xylanase by Thermomyces lanuginosus d) cultivation of Tetrahymena thermophila in 1.5 bioreactors, e) alginate production by Azotobacter vine-landii. 

In addition to cutinases, various lipases, such as from C. antarctica, Candida sp. [13, 47], Thermomyces lanuginosus [2, 14, 15, 55, 56], Burkholderia (formerly Pseudomonas) cepacia [57] and esterases from Pseudomonas sp. (serine esterase) [58] and Bacillus sp. (nitrobenzyl esterases) [59, 60], have shown PET hydrolase... 

Other microbial lipases have also been successfully used in anhydrous ionic liquids, e.g., from Alcaligenes sp. (AsL) [54, 58], CaLA, Rhizomucor miehei lipase (RmL), and Thermomyces lanuginosus lipase (TIL) [54]. The lipase from pig pancreas (porcine pancreas lipase, PPL), the only mammalian lipase that has been subjected to ionic liquids, catalyzed transesterificationin[BMIm][NTf2]butnotin[BMIm][PF6]... 

TIL Thermomyces lanuginosus lipase, RdL Rhizopus delemar lipase, RnL Rhizopus niveus lipase, MmE Mucor miehei esterase, PsL Pseudomonas sp. lipase, MmL Mucor miehei lipase, RoL Rhizopus orvzae lipase, CaLA Candida antarctica lipase A, CaLB Candida antarctica lipase B, PLE Pig liver esterase, EP Enteropeptidase, PKA Porcine kidney acylase, CE Cholesterol esterase Figure 8.1 (S)-Selective enzyme hits from hydrolase screening. ... 

As an alternative to the chemical resolution methods described by Atwal et al. (Scheme 4.13), a biocatalytic strategy towards the preparation of enantiopure (R) and (S)-SQ 32,926 was developed (Scheme 4.15). The key step in the synthesis is the enzymatic resolution of an N3-acetoxymethyl-activated dihydropyrimidone precursor by Thermomyces lanuginosus lipase [189]. The readily available racemic DHPM 43 was hydroxymethylated at N3 with formaldehyde, followed by standard acetylation with acetyl chloride. The resulting N3-acetoxymethyl-activated DHPM... 

Application of Xylanase from Thermomyces lanuginosus IOC-4145 for Enzymatic Hydrolysis of Corncob and Sugarcane Bagasse... 

Index Entries Xylanase Thermomyces lanuginosus agricultural residues enzymatic hydrolysis corncob sugarcane bagasse. 

Lin, J., Ndlovu, L. M., Singh, S., and Pillay, B., Purification and biochemical characteristics of beta-D-xylanase from a thermophilic fungus, Thermomyces lanuginosus-SSBP. Biotechnol Appl Biochem 1999, 30 (Pt 1), 73-9. 

Yin E, Le YL, Pei JJ, Shao WL, Yang QY (2008) High-level expression of the xylanase from Thermomyces lanuginosus in Escherichia coli. World J Microbiol Biotechnol 24 275-280... 

Three different variants of Thermomyces lanuginosus lipase (TLL) were used as the model enzyme to study the hydrolysis of the phopsholipid bilayer. Being a lipase, TLL has low affinity for phospholipid bilayers [39,40]. TLL is, therefore, of interest for the characterization of the diffusion and adsorption... 

High molecular weight poly(trimethylene carbonate) PTMC (Mn 300 k g/mol, Mw/Mn 1.46), synthesized, purified, and characterized as described in reference [72] is dissolved in chloroform (3 mg/mL). Thin films are prepared by spin-coating these solutions on cleaned Si wafers at 3,000 rpm (film thickness obtained 25 50 nm). Film thicknesses can be determined by AFM imaging using the scratch method described in Chap. 2 (see also above, hands-on example 47). The enzymatic reaction takes place in situ in the liquid cells filled with lipase solutions (lipase from Thermomyces lanuginosus (EC3.1.1.3, minimum 50,000 units/g purchased from Sigma, U.S.A.) at 37°C for 30 s, 1 min, and 2 min, respectively. 

The application of ionic liquids in lipase biocatalysis has not remained entirely restricted to CaLB, PcL or CrL. Other lipases have been used in ionic liquids for ester synthesis such as Candida antarctica lipase A (CaLA) [15,16], Thermomyces lanuginosus lipase [17] (TLL), Rhizomucor miehei lipase (PmL), Pseudomonas fluorescens lipase (PJL) [18], Pig pancreas lipase (PpL) [17] and Alcaligenes sp. lipase (A5 L) [16]. 

Thermomyces lanuginosus Depilling assay, release of oligomers, hydrophilicity, XPS, Maldi-Tof, K/S values after dying, FTIR, surface derivatization [24, 52-56]... 

In this work, MG and DG are produced through lipase-catalyzed glycerolysis of soybean oil in a batch reactor using Candida antarctica B, Thermomyces lanuginosus, Rhizomucor miehei, Candida rugosa, and Aspergillus niger lipases, in a solvent-free system. 

Chirazyme L2-C2 (CAL-B) proved to be a very useful enzyme for the development of an acylation process for the large-scale production of vitamin A (retinol, 91) at Roche (Scheme 27) [90,91]. In the plant process of vitamin A, intermediate 88 is partially acylated and then subjected to acid-catalyzed dehydration and isomerization to yield the vitamin A ester 90 via acetate 89. Contrary to the chemical acylation, an enzymatic approach allowed for a highly selective monoacylation of 88, and Chirazyme L2-C2 showed a very high conversion rate at 30% (w/w) substrate concentration. A first continuous process on the laboratory scale was set up with a 15 ml fixed-bed reactor containing 5.0-8.0 g of immobilized biocatalyst 4.9 kg of 89 was synthesized within 100 days in 99% yield and with 97% selectivity for the primary hydroxyl group. The laboratory process was implemented in a miniplant (120 g of biocatalyst), which could convert 1.4 kg of 88 into 1.6 kg 89 per day. After 74 days the conversion efficiency was still 99.4%. Further development of this transformation led to a modified process, which uses Thermomyces lanuginosus lipase immobilized on Accurel MPlOOl for the continuous production of 89 [92]. 

The properties of a thermostable glucoamylase from a thermophilic fungus Thermomyces lanuginosus have been examined. 

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