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Article: Chemical modification of carboxyl groups in porcine pepsin

TitleChemical modification of carboxyl groups in porcine pepsin
Authors
Issue Date1980
PublisherAmerican 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?
AbstractModification 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 Identifierhttp://hdl.handle.net/10722/178411
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorNakai, Sen_US
dc.date.accessioned2012-12-19T09:47:34Z-
dc.date.available2012-12-19T09:47:34Z-
dc.date.issued1980en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 1980, v. 28 n. 4, p. 834-839en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178411-
dc.description.abstractModification 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.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_US
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_US
dc.titleChemical modification of carboxyl groups in porcine pepsinen_US
dc.typeArticleen_US
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_US
dc.identifier.authorityMa, CY=rp00759en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0019042330en_US
dc.identifier.volume28en_US
dc.identifier.issue4en_US
dc.identifier.spage834en_US
dc.identifier.epage839en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridNakai, S=7201877285en_US

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