{alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

Publication Date:
2018-11-29
Publisher:
Royal Society
Electronic ISSN:
2054-5703
Topics:
Natural Sciences in General
Keywords:
biochemistry, biomaterials
Published by:
http://royalsocietypublishing.org/
_version_ 1839208237213155328
autor Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
beschreibung Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. α-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble α-amylase was shifted from 6.0 to 6.5. The immobilized α-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble α-amylases were 9.6 and 3.8 mg starch ml –1 , respectively. In conclusion, this method shows that the immobilized α-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.
citation_standardnr 6362095
datenlieferant ipn_articles
feed_id 220702
feed_publisher Royal Society
feed_publisher_url http://royalsocietypublishing.org/
insertion_date 2018-11-29
journaleissn 2054-5703
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher Royal Society
quelle Royal Society Open Science
relation http://rsos.royalsocietypublishing.org/cgi/content/short/5/11/172164?rss=1
schlagwort biochemistry, biomaterials
search_space articles
shingle_author_1 Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
shingle_author_2 Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
shingle_author_3 Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
shingle_author_4 Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
shingle_catch_all_1 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
biochemistry, biomaterials
Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. α-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble α-amylase was shifted from 6.0 to 6.5. The immobilized α-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble α-amylases were 9.6 and 3.8 mg starch ml –1 , respectively. In conclusion, this method shows that the immobilized α-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.
Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
Royal Society
2054-5703
20545703
shingle_catch_all_2 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
biochemistry, biomaterials
Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. α-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble α-amylase was shifted from 6.0 to 6.5. The immobilized α-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble α-amylases were 9.6 and 3.8 mg starch ml –1 , respectively. In conclusion, this method shows that the immobilized α-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.
Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
Royal Society
2054-5703
20545703
shingle_catch_all_3 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
biochemistry, biomaterials
Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. α-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble α-amylase was shifted from 6.0 to 6.5. The immobilized α-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble α-amylases were 9.6 and 3.8 mg starch ml –1 , respectively. In conclusion, this method shows that the immobilized α-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.
Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
Royal Society
2054-5703
20545703
shingle_catch_all_4 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
biochemistry, biomaterials
Enzyme immobilization is one of the most important techniques for industrial applications. It makes the immobilized enzyme more stable and advantageous than the free form in different aspects. α-Amylase was immobilized on 4% cyanuric chloride-activated amidoximated acrylic fabric at pH 7.0 with (79%) maximum efficiency. A field emission scanning electron microscope and Fourier transform infrared were used to confirm the immobilization process. Even after being recycled 10 times, the immobilized enzyme lost just 28% of its initial activity. Owing to immobilization, the pH of the soluble α-amylase was shifted from 6.0 to 6.5. The immobilized α-amylases showed thermal stability at 60°C, and became more resistant to heavy metal ions. The k m values of the immobilized and soluble α-amylases were 9.6 and 3.8 mg starch ml –1 , respectively. In conclusion, this method shows that the immobilized α-amylase proved to be more efficient than its soluble form, and hence could be used during saccharification of starch.
Almulaiky, Y. Q., Aqlan, F. M., Aldhahri, M., Baeshen, M., Khan, T. J., Khan, K. A., Afifi, M., AL-Farga, A., Warsi, M. K., Alkhaled, M., Alayafi, A. A. M.
Royal Society
2054-5703
20545703
shingle_title_1 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
shingle_title_2 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
shingle_title_3 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
shingle_title_4 {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
timestamp 2025-07-31T23:47:38.149Z
titel {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
titel_suche {alpha}-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride
topic TA-TD
uid ipn_articles_6362095