Cutinase-like enzyme

Recently, the production of a biodegradable plastic-degrading enzyme from cheese whey by the phyllosphere yeast Pseudozyma antartica GB-4(1)W was studied [25]. It was reported that this yeast produces a cutinase-like enzyme, PaE, which has the ability to degrade biodegradable plastics. This enzyme was reported to have the ability to degrade several bioplastics such as PBS, polybutylene succinate-co-adipate, poly(e-caprolactone) and polylactic acid. Fed-batch cultivation of this yeast in xylose resulted in the production of PaE with high productivity. 

Masaki, K., Kamini, N.R., and Ikeda, H. (2005) Cutinase-like enzyme from the yeast Cryptococcus sp. strain S-2 hydrolyzes polylactic acid and other biodegradable plastics. Appi Environ. Microbiol, 71, 7548-7550. 

An MD study of an enzyme, the serine protease cutinase from Fusarium solani pisi, in [C4mim][PF6] and [C4mim][N03] was presented. The authors observed an enzyme structure that is dependent on the amount of water present in the IL [124], They showed that the enzyme is preferentially stabilized in [C4mim][PF6] at 5-10 wt% (weight of water over protein) water content at 298 K. [C4mim][PF6] rendered a more native-like enzyme structure at the same water content of 5—10 wt% as... 

Mica81o and Soares [105] reported for the first time a molecular simulation study of the serine protease cutinase from Fusarium solani in two ILs, [bmimjPF and [bmimjNOj. It was found that the enzyme structure is highly dependent on the amount of water present in the IL media and that the protein seems to display structural properties following a bell-shape-like behavior relative to the amount of water present in the system. ILs can interact with protein molecules, and this interaction is governed by the affinity of anions toward the protein main chain. 

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