MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES
Starch degrading enzymes are used as feed additives to increase the digestibility of corn meal based diet in livestock and poultry. To be efficient, these enzymes have to present a good activity and stability. Immobilization by physical bonding o f enzymes on a porous support is a simple and efficie...
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| Format: | Article |
| Language: | English |
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Agroprint Timisoara
2023-10-01
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| Series: | Scientific Papers Animal Science and Biotechnologies |
| Subjects: | |
| Online Access: | https://spasb.ro/index.php/public_html/article/view/1182 |
| _version_ | 1797215546224148480 |
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| author | MONICA DRAGOMIRESCU T. VINTILĂ GABRIELA PREDA |
| author_facet | MONICA DRAGOMIRESCU T. VINTILĂ GABRIELA PREDA |
| author_sort | MONICA DRAGOMIRESCU |
| collection | DOAJ |
| description | Starch degrading enzymes are used as feed additives to increase the digestibility of
corn meal based diet in livestock and poultry. To be efficient, these enzymes have to
present a good activity and stability. Immobilization by physical bonding o f enzymes
on a porous support is a simple and efficient method to preserve enzyme molecules
in an active form and retain their activity for a period o f time.
The aim o f this study was to stabilize an enzymatic preparation with amylase activity
produced by a native strain o f Bacillus amyloliquefaciens in submerged culture. The
immobilization technique used was physical bonding on a porous ceramic support.
The enzymatic preparation with amylase activity was used in immobilization in a
liophylized form. By using the same method we immobilized also a purified
Aspergillus niger amylase. For both enzymes, the optimal temperature and pH o f the
native and immobilized enzymes did not vary significantly. At temperature and pH
values lower than the optimum, the relative activities have been higher for the
immobilized Bacillus amyloliquefaciens enzyme compared to the native one. The
immobilization has led to an enzymatic compound with stability at pH 3 and 37°C
and in time higher than that o f the free one. |
| first_indexed | 2024-04-24T11:31:47Z |
| format | Article |
| id | doaj.art-2e62f395d62840daa6b0b97b7ff3bb4c |
| institution | Directory Open Access Journal |
| issn | 1841-9364 2344-4576 |
| language | English |
| last_indexed | 2024-04-24T11:31:47Z |
| publishDate | 2023-10-01 |
| publisher | Agroprint Timisoara |
| record_format | Article |
| series | Scientific Papers Animal Science and Biotechnologies |
| spelling | doaj.art-2e62f395d62840daa6b0b97b7ff3bb4c2024-04-10T08:31:31ZengAgroprint TimisoaraScientific Papers Animal Science and Biotechnologies1841-93642344-45762023-10-0142135351182MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICESMONICA DRAGOMIRESCU0T. VINTILĂ1GABRIELA PREDA2Faculty o f Animal Sciences and Biotechnologies, Timişoara, România,Faculty o f Animal Sciences and Biotechnologies, Timişoara, RomâniaFaculty o f Chemistry-Biology-Geography, Timişoara, RomâniaStarch degrading enzymes are used as feed additives to increase the digestibility of corn meal based diet in livestock and poultry. To be efficient, these enzymes have to present a good activity and stability. Immobilization by physical bonding o f enzymes on a porous support is a simple and efficient method to preserve enzyme molecules in an active form and retain their activity for a period o f time. The aim o f this study was to stabilize an enzymatic preparation with amylase activity produced by a native strain o f Bacillus amyloliquefaciens in submerged culture. The immobilization technique used was physical bonding on a porous ceramic support. The enzymatic preparation with amylase activity was used in immobilization in a liophylized form. By using the same method we immobilized also a purified Aspergillus niger amylase. For both enzymes, the optimal temperature and pH o f the native and immobilized enzymes did not vary significantly. At temperature and pH values lower than the optimum, the relative activities have been higher for the immobilized Bacillus amyloliquefaciens enzyme compared to the native one. The immobilization has led to an enzymatic compound with stability at pH 3 and 37°C and in time higher than that o f the free one.https://spasb.ro/index.php/public_html/article/view/1182feed enzymesamylasebacillus amyloliquefaciensaspergillus nigerstabilizationphysical bonding |
| spellingShingle | MONICA DRAGOMIRESCU T. VINTILĂ GABRIELA PREDA MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES Scientific Papers Animal Science and Biotechnologies feed enzymes amylase bacillus amyloliquefaciens aspergillus niger stabilization physical bonding |
| title | MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES |
| title_full | MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES |
| title_fullStr | MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES |
| title_full_unstemmed | MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES |
| title_short | MICROBIAL HYDROLASES IMMOBILIZED ON POROUS MATRICES |
| title_sort | microbial hydrolases immobilized on porous matrices |
| topic | feed enzymes amylase bacillus amyloliquefaciens aspergillus niger stabilization physical bonding |
| url | https://spasb.ro/index.php/public_html/article/view/1182 |
| work_keys_str_mv | AT monicadragomirescu microbialhydrolasesimmobilizedonporousmatrices AT tvintila microbialhydrolasesimmobilizedonporousmatrices AT gabrielapreda microbialhydrolasesimmobilizedonporousmatrices |