File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Scopus: eid_2-s2.0-0019042330
- WOS: WOS:A1980JZ82100034
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Chemical modification of carboxyl groups in porcine pepsin
Title | Chemical modification of carboxyl groups in porcine pepsin |
---|---|
Authors | |
Issue Date | 1980 |
Publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau |
Citation | Journal Of Agricultural And Food Chemistry, 1980, v. 28 n. 4, p. 834-839 How to Cite? |
Abstract | Modification of up to 11 carboxyl groups in porcine pepsin with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide and glycine methyl ester caused changes in activities, specificity, and physicochemical properties of the enzyme. The milk clotting activity was markedly decreased to 10%, while the proteolytic activity was not affected. The decrease in the peptidase activity was about 50%. The charge density of pepsin decreased upon modification, as shown in a decrease of relative electrophoretic mobility and in a shift of pH optimum from 2 to 3.5. Kinetic studies showed that K m was increased, while k cat was not significantly affected. The presence of dipeptide substrates interfered with the modification. The modified pepsin remained reactive to two site-specific pepsin inhibitors. These effects of carboxyl modification were not unique to pepsin; modification of carboxyl groups caused similar changes in the activities and properties of pepsinogen and chymosin. The stability of the modified pepsin near neutral pH was considerably improved, suggesting that the modified enzyme may be a more suitable rennet substitute than native pepsin in cheese-making. © 1980 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/178411 |
ISSN | 2023 Impact Factor: 5.7 2023 SCImago Journal Rankings: 1.114 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ma, CY | en_US |
dc.contributor.author | Nakai, S | en_US |
dc.date.accessioned | 2012-12-19T09:47:34Z | - |
dc.date.available | 2012-12-19T09:47:34Z | - |
dc.date.issued | 1980 | en_US |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 1980, v. 28 n. 4, p. 834-839 | en_US |
dc.identifier.issn | 0021-8561 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178411 | - |
dc.description.abstract | Modification of up to 11 carboxyl groups in porcine pepsin with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide and glycine methyl ester caused changes in activities, specificity, and physicochemical properties of the enzyme. The milk clotting activity was markedly decreased to 10%, while the proteolytic activity was not affected. The decrease in the peptidase activity was about 50%. The charge density of pepsin decreased upon modification, as shown in a decrease of relative electrophoretic mobility and in a shift of pH optimum from 2 to 3.5. Kinetic studies showed that K m was increased, while k cat was not significantly affected. The presence of dipeptide substrates interfered with the modification. The modified pepsin remained reactive to two site-specific pepsin inhibitors. These effects of carboxyl modification were not unique to pepsin; modification of carboxyl groups caused similar changes in the activities and properties of pepsinogen and chymosin. The stability of the modified pepsin near neutral pH was considerably improved, suggesting that the modified enzyme may be a more suitable rennet substitute than native pepsin in cheese-making. © 1980 American Chemical Society. | en_US |
dc.language | eng | en_US |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau | en_US |
dc.relation.ispartof | Journal of Agricultural and Food Chemistry | en_US |
dc.title | Chemical modification of carboxyl groups in porcine pepsin | en_US |
dc.type | Article | en_US |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_US |
dc.identifier.authority | Ma, CY=rp00759 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.scopus | eid_2-s2.0-0019042330 | en_US |
dc.identifier.volume | 28 | en_US |
dc.identifier.issue | 4 | en_US |
dc.identifier.spage | 834 | en_US |
dc.identifier.epage | 839 | en_US |
dc.identifier.isi | WOS:A1980JZ82100034 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.scopusauthorid | Nakai, S=7201877285 | en_US |
dc.identifier.issnl | 0021-8561 | - |