New model substrates for enzymes hydrolysing polyethyleneterephthalate and polyamide fibres.
نویسندگان
چکیده
Recently the potential of enzymes for surface hydrophilisation and/or functionalisation of polyethyleneterephthalate (PET) and polyamide (PA) has been discovered. However, there was no correlation between enzyme class/activity (e.g. esterase, lipase, cutinase) and surface hydrolysis of these polymers and consequently no simple assay to estimate this capability. Enzymes active on the model substrates bis (benzoyloxyethyl) terephthalate and adipic acid bishexyl-amide, were also capable of increasing the hydrophilicity of PET and PA. When dosed at the identical activity on 4-nitrophenyl butyrate, only enzymes from Thermobifida fusca, Aspergillus sp., Beauveria sp. and commercial enzymes (TEXAZYME PES sp5 and Lipase PS) increased the hydrophilicity of PET fibres while other esterases and lipases did not show any effect. Activity on PET correlated with the activity on the model substrate. Hydrophilicity of fibres was greatly improved based on increases in rising height of up to 4.3 cm and the relative decrease of water absorption time between control and sample of the water was up to 76%. Similarly, enzymes increasing the hydrophilicity of PA fibres such as from Nocardia sp., Beauveria sp. and F. solani hydrolysed the model substrate; however, there was no common enzyme activity (e.g. protease, esterase, amidase) which could be attributed to all these enzymes.
منابع مشابه
Biotransformations in synthetic fibres
Recent studies clearly indicate that the modification of synthetic polymers with enzymes is an environmentally friendly alternative to traditional chemical methods requiring harsh conditions. Some work already performed on polyamide 6.6 (nylon 6.6), polyethyleneterephthalate (PET) and polyacrylonitrile (PAN) revealed that surface functionalization of these materials is a key requirement for an ...
متن کاملSCREENING FOR STARCH-HYDROLYSING BACTERIA
Screening of3000 soil samples collected from cities of four different provinces of Iran for starch-hydrolysing bacteria revealed that the nature is enriched with Streptomyces species capable of producing amylolytic enzymes. Among the bacterial isolates, one of the high starch-degrading strains was selected for further microbiological identification and also amylolytic enzyme(s) characteriza...
متن کاملImproved Fastness Properties of some Novel Triarylmethane Dyes on Acrylic Fibres
In this research, several series of triarylmethane dyes containing one or more terminal methoxy substituents with a variable tertiary amino groups have been used. These dyes have been applied to different substrates by using various methods including transfer printing and then their fastness properties were measured. These dyes shows exceptionally high light fastness (6-7) on acid modified poly...
متن کاملStudies on the nature of silicosis: a suggested mechanism of fibrogenesis.
One theory which seeks to explain the production of fibrous tissue in silicosis postulates the interaction of collagen precursors with polysilicic acid. This stage has been questioned because it is doubtful whether polymerized silicic acid is normally formed when quartz dissolves in aqueous media. A mechanism by which silicic acid may be polymerized in vivo has been demonstrated by studying the...
متن کاملFragrance release from the surface of branched poly (amide)s.
Enzymes are powerful tools in organic synthesis that are able to catalyse a wide variety of selective chemical transformations under mild and environmentally friendly conditions. Enzymes such as the lipases have also found applications in the synthesis and degradation of polymeric materials. However, the use of these natural catalysts in the synthesis and the post-synthetic modification of dend...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of biochemical and biophysical methods
دوره 69 1-2 شماره
صفحات -
تاریخ انتشار 2006