IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS

In this study, polyamide 6 polymer surfaces that have a high surface area were produced by electrospinning method with the participation of Glycine, Tyrosine and Glutamic acid amino acids, and lyophilized Bacillus subtilis E6-5 protease and commercial protease enzymes were immobilized on nanofibrils...

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Main Authors: Elif Demi̇rkan, Tuba Sevgi̇, Baran Enes Guler
Format: Article
Language:English
Published: Trakya University 2020-04-01
Series:Trakya University Journal of Natural Sciences
Subjects:
Online Access:https://dergipark.org.tr/en/pub/trkjnat/issue/53613/633788
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spelling doaj-36b773e8ef2d453eb0267bde79769cd22021-01-20T12:52:04ZengTrakya UniversityTrakya University Journal of Natural Sciences2147-02942528-96912020-04-01211394510.23902/trkjnat.63378869IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDSElif Demi̇rkan0Tuba Sevgi̇1Baran Enes Guler2ULUDAĞ ÜNİVERSİTESİULUDAĞ ÜNİVERSİTESİULUDAĞ ÜNİVERSİTESİIn this study, polyamide 6 polymer surfaces that have a high surface area were produced by electrospinning method with the participation of Glycine, Tyrosine and Glutamic acid amino acids, and lyophilized Bacillus subtilis E6-5 protease and commercial protease enzymes were immobilized on nanofibrils. Enzyme reusability were investigated. The immobilization efficiencies of the enzymes were approximately between 50-55 %. In studies with lyophilized Bacillus protease, glutaraldehyde activated PA6 nanofibrils and glutaraldehyde unactivated PA6 nanofibrils were found to be more immobilized in the presence of Glutamic acid. Although the lyophilized protease enzyme immobilized on non-glutaraldehyde activated and activated surfaces has been used 4 times, the best functional stability has been achieved with 2 times use. In pure PA6/Glutamic acid nanofibrils, the immobilization yield of the two times used enzymes was found to be 38 %. In glutaraldehyde-activated PA6 nanofibrils, the PA6/Glutamic acid nanofibril surfaces were found to have 65 % immobilization yield of the two repetitive used enzymes. The enzyme immobilization efficiency has been doubled by glutaraldehyde activation of the nanofibrils. In studies with commercial protease, the most functional stability was obtained for 3 repeated uses, although the enzyme was used 6 times on the non-glutaraldehyde activated nanofibril surfaces. The most successful immobilization was found in 58 % of PA6 nanofibrils. In glutaraldehyde-activated PA6 nanofibrils, the enzyme was found to be used 6 times, but the functional stability was maintained as much as 4 times of repeated use.https://dergipark.org.tr/en/pub/trkjnat/issue/53613/633788immobilizationelektrospinnigproteasereusability
collection DOAJ
language English
format Article
sources DOAJ
author Elif Demi̇rkan
Tuba Sevgi̇
Baran Enes Guler
spellingShingle Elif Demi̇rkan
Tuba Sevgi̇
Baran Enes Guler
IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS
Trakya University Journal of Natural Sciences
immobilization
elektrospinnig
protease
reusability
author_facet Elif Demi̇rkan
Tuba Sevgi̇
Baran Enes Guler
author_sort Elif Demi̇rkan
title IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS
title_short IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS
title_full IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS
title_fullStr IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS
title_full_unstemmed IMMOBILIZATION OF Bacillus subtilis E6-5 PROTEASE AND COMMERCIAL PROTEASE IN NANOFIBRILS CONTAINING DIFFERENT AMINO ACIDS
title_sort immobilization of bacillus subtilis e6-5 protease and commercial protease in nanofibrils containing different amino acids
publisher Trakya University
series Trakya University Journal of Natural Sciences
issn 2147-0294
2528-9691
publishDate 2020-04-01
description In this study, polyamide 6 polymer surfaces that have a high surface area were produced by electrospinning method with the participation of Glycine, Tyrosine and Glutamic acid amino acids, and lyophilized Bacillus subtilis E6-5 protease and commercial protease enzymes were immobilized on nanofibrils. Enzyme reusability were investigated. The immobilization efficiencies of the enzymes were approximately between 50-55 %. In studies with lyophilized Bacillus protease, glutaraldehyde activated PA6 nanofibrils and glutaraldehyde unactivated PA6 nanofibrils were found to be more immobilized in the presence of Glutamic acid. Although the lyophilized protease enzyme immobilized on non-glutaraldehyde activated and activated surfaces has been used 4 times, the best functional stability has been achieved with 2 times use. In pure PA6/Glutamic acid nanofibrils, the immobilization yield of the two times used enzymes was found to be 38 %. In glutaraldehyde-activated PA6 nanofibrils, the PA6/Glutamic acid nanofibril surfaces were found to have 65 % immobilization yield of the two repetitive used enzymes. The enzyme immobilization efficiency has been doubled by glutaraldehyde activation of the nanofibrils. In studies with commercial protease, the most functional stability was obtained for 3 repeated uses, although the enzyme was used 6 times on the non-glutaraldehyde activated nanofibril surfaces. The most successful immobilization was found in 58 % of PA6 nanofibrils. In glutaraldehyde-activated PA6 nanofibrils, the enzyme was found to be used 6 times, but the functional stability was maintained as much as 4 times of repeated use.
topic immobilization
elektrospinnig
protease
reusability
url https://dergipark.org.tr/en/pub/trkjnat/issue/53613/633788
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AT tubasevgi immobilizationofbacillussubtilise65proteaseandcommercialproteaseinnanofibrilscontainingdifferentaminoacids
AT baranenesguler immobilizationofbacillussubtilise65proteaseandcommercialproteaseinnanofibrilscontainingdifferentaminoacids
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