Direct enzymatic esterification of cotton and Avicel with wild-type and engineered cutinases

Abstract

In this work, the surface of cellulose, either Avicel or cotton fabric, was modified using cutinases without any previous treatment to swell or to solubilise the polymer. Aiming further improvement of cutinase ester synthase activity on cellulose, an engineered cutinase was investigated. Wild-type cutinase from Fusarium solani and its fusion with the carbohydratebinding module N1 from Cellulomonas fimi were able to esterify the hydroxyl groups of cellulose with distinct efficiencies depending on the acid substrate/ solvent system used, as shown by titration and by ATR-FTIR. The carbonyl stretching peak area increased significantly after enzymatic treatment during 72 h at 30°C. Cutinase treatment resulted in relative increases of 31 and 9 % when octanoic acid and vegetable oil were used as substrates, respectively. Cutinase-N1 treatment resulted in relative increases of 11 and 29 % in the peak area when octanoic acid and vegetable oil were used as substrates, respectively. The production and application of cutinase fused with the domain N1 as a cellulose ester synthase, here reported for the first time, is therefore an interesting strategy to pursuit.

Cutinase promotes dry esterification of cotton cellulose

“…The most important absorption peaks at 1745 and 1748 cm −1 were assigned to the C=O stretching and vibration, respectively, for cotton treated with active cutinase. The peak position depends on several factors like the position of the esterification carbon in the glycoside . The absorption peak at 1745 cm −1 for cotton treated with active cutinase was significantly stronger (56% of increase in peak area) than that for the control sample.…”

“…The peak position depends on several factors like the posi-tion of the esterification carbon in the glycoside. 9 The absorption peak at 1745 cm 21 for cotton treated with active cutinase was significantly stronger (56% of increase in peak area) than that for the control sample. After subtracting the control spectrum, the resulting curve (Figure 4 curve C) showed a prominent peak at 1745 cm 21 .…”

“…The heterogeneous esterification of macroscopic and microscopic cellulose using enzymes, mainly cutinase and lipases, is reported by few groups. 19,23 Only plain woven cotton was used as substrate for cutinase-mediated esterification by Matama et al 9 In this work we present a new approach for the simple and direct biomodification of hydroxyl groups on the surface of cotton fabric cellulose-a solvent-free process, using cutinase from T. fusca, which presents a higher thermal stability than cutinase from F. solani. Using the methodology here reported and using an important control-inactivated cutinase, we demonstrated that the time to completely absorb a drop of water on the cutinase-treated cotton fabric was significantly increased compared to the control.…”

“…This versatile catalytic ability of cutinase is also described in a wide range of fiber modifications like wool anti‐felting, cotton bio‐scouring, and even synthetic fibers modification . The enzymatic esterification of Avicel and cotton cellulose was reported using wild‐type cutinase from Fusarium solani and an engineered cutinase, fused with the carbohydrate‐binding module N1 from Cellolomonas fimi . The surface esterification of hemicellulose films catalyzed by lipases from Mucor javanicus , Rhizopus oryzae , Candida rugosa and by a cutinase from F. solani pisi is reported by others .…”

Enzymatic coating of cotton with poly (ethylene glutarate)

“…Despite the presence of 25% of water (v/v) in the intial reaction mixture, which usually inhibits transesterification, the reaction took place resulting in the formation of several oligomeric products. A soluble lipase was used to coat the fibre because the enzyme in a solid support enzyme would not promote in situ polymerization [26] and [30].…”