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Humicola insolens cutinase

Fig. 3 Top row. Hydrolysis of PET with 7% crystallinity with a Humicola insolens cutinase for (a) 0, (b) 12 and (c) 48 h resulting in weight losses of 0, 18% and 54%, respectively. Bottom row. Hydrolysis of PET with (a) 34.8% crystallinity (blank), (b) a lipolytic enzyme (no weight loss) and (c) 1 M NaOH (modified from [14, 18])... Fig. 3 Top row. Hydrolysis of PET with 7% crystallinity with a Humicola insolens cutinase for (a) 0, (b) 12 and (c) 48 h resulting in weight losses of 0, 18% and 54%, respectively. Bottom row. Hydrolysis of PET with (a) 34.8% crystallinity (blank), (b) a lipolytic enzyme (no weight loss) and (c) 1 M NaOH (modified from [14, 18])...
The polymerization of substrates varying in a,(o-n-alkane diol and a,co- -alkane diacid chain length by Humicola insolens cutinase immobilized on Amberzyme oxiranes (HiC-AO) and Novozym 435 was studied [39], HIC-AO... [Pg.93]

Apart from CALB other enzymes were shown to be able to successfully polymerize lactones. For instance Lipase PS-30, immobilized on Celite, was used as catalyst to study PDL-ROP under bulk reaction conditions. Poly(PDL) with M = 62000 and PDI 1.9 was reported [76]. Gross and coworkers could show that Humicola insolens cutinase (HiC) showed a high catalytic activity for enzymatic ROP of e-CL and PDL [87]. Poly(e-CL) with M n = 16000 (M /lVf = 3.1), in >99% yields was produced in bulk (70 °C, 24h) with 0.1% w/w immobilized HiC. Furthermore, using immobilized HiC in toluene (70 °C, 24h), PDL was converted to poly(PDL) (99% yield) with M = 44600 and Mw/M = 1.7. [Pg.107]

Humicola insolens cutinase immobilized on Amberzyme oxiranes... [Pg.461]

Diacids (succinic acid, adipic acid, suberic acid, and sebacic acid), diols (cyclohexane-1,4-dimethanol, 1,8-octanediol, 1,6-hexanediol and 1,4-butane-diol), and lactone (co-pentadecalactone) were purchased from Aldrich Chemical Co. in the highest available purity and used as received m-Caprolactone, a gift from Union Carbide, was dried over calcium hydride and distilled under reduced pressure in a nitrogen atmosphere. Humicola insolens cutinase was a gift from Novozymes (Bagsvaerd, Denmark). Lewatit OC VOC 1600 was received as a gift from Rohm and Haas. [Pg.269]

A. D. Nielsen, L. Arleth, and P. Westh, Analysis of protein-surfactant interactions—a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant, Biochimica et Biophysica Acta, vol. 1752, no. 2, pp. 124—132, 2005. [Pg.89]

As described by Hunsen and co-workers [31], cutinase HiC (cutin hydrolase from Humicola insolens) catalysed a dehydration polycondensation between a glycol and a diacid at 70 °C for 48 h under vacuum, containing 1 % w/w enzyme. With the adipic acid component fixed, polyesters with M values up to 12,000 Da were obtained from diols. With the 1,4-cyclohexanedimethanol component fixed, polyesters obtained from succinic acid, adipic acid, suberic acid and sebacic acid had Mn values of 900, 4,000, 5,000 and 19,000 Da, respectively. [Pg.432]


See other pages where Humicola insolens cutinase is mentioned: [Pg.87]    [Pg.461]    [Pg.263]    [Pg.270]    [Pg.270]    [Pg.87]    [Pg.461]    [Pg.263]    [Pg.270]    [Pg.270]    [Pg.120]    [Pg.372]    [Pg.268]    [Pg.113]    [Pg.183]   
See also in sourсe #XX -- [ Pg.87 , Pg.90 , Pg.93 , Pg.107 , Pg.305 , Pg.330 , Pg.373 ]

See also in sourсe #XX -- [ Pg.266 ]




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