Studies on activity, distribution, and zymogram of protease, α-amylase, and lipase in the paddlefish Polyodon spathula.
Identifieur interne : 000399 ( Ncbi/Curation ); précédent : 000398; suivant : 000400Studies on activity, distribution, and zymogram of protease, α-amylase, and lipase in the paddlefish Polyodon spathula.
Auteurs : H. Ji [République populaire de Chine] ; H T Sun ; D M XiongSource :
- Fish physiology and biochemistry [ 1573-5168 ] ; 2012.
English descriptors
- KwdEn :
- MESH :
- chemical , classification : Peptide Hydrolases.
- chemical , metabolism : Lipase, Peptide Hydrolases, alpha-Amylases.
- metabolism : Carps, Fishes.
- physiology : Digestion, Fishes.
- Animal Feed, Animals, Hydrogen-Ion Concentration, Kinetics, Species Specificity.
Abstract
A series of biochemical determination and electrophoretic observations have been conducted to analyze the activities and characteristics of protease, α-amylase, and lipase of paddlefish Polyodon spathula. The results obtained have been compared with those of bighead carp (Aristichthys nobilis) and hybrid sturgeon (Huso dauricus ♀ × Acipenser schrenki Brandt ♂), in order to increase available knowledge of the physiological characteristics of this sturgeon species and to gain information with regard to its nutrition. Further, a comparative study of enzymatic activity, distribution, and characterization between commercial feed-reared paddlefish (CG) and natural live food-reared (NG) paddlefish was conducted. Results showed that higher proteolytic activity was observed in the pH range 2.5-3.0 and at a pH of 7.0 for paddlefish. Levels of acid protease activity of paddlefish were similar to that of hybrid sturgeon, and significantly higher than that of bighead carp. The inhibition assay of paddlefish showed that the rate of inhibition of tosyl-phenylalanine chloromethyl ketone was approximately 2.6-fold that of tosyl-lysine chloromethyl ketone. There was no significant difference observed for acid protease activity between PG and CG groups, whereas the activity of alkaline protease, α-amylase, and lipase in the PG group were significantly lower than those in the CG group. The substrate sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis further showed that there were certain types of enzymes, especially α-amylase, with similar molecular mass in the paddlefish and hybrid sturgeon. It can be inferred that acid digestion was main mechanism for protein hydrolysis in paddlefish, as reported for other fishes with a stomach. This indicates that the paddlefish requires higher alkaline protease, α-amylase, and lipase activity to digest natural live food.
DOI: 10.1007/s10695-011-9541-9
PubMed: 21894570
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Ji</name><affiliation wicri:level="1"><nlm:affiliation>College of Animal Science and Technology, Northwest A & F University, Yangling, China. jihong0405@hotmail.com</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Animal Science and Technology, Northwest A & F University, Yangling</wicri:regionArea><wicri:noRegion>Yangling</wicri:noRegion></affiliation></author><author><name sortKey="Sun, H T" sort="Sun, H T" uniqKey="Sun H" first="H T" last="Sun">H T Sun</name></author><author><name sortKey="Xiong, D M" sort="Xiong, D M" uniqKey="Xiong D" first="D M" last="Xiong">D M Xiong</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:21894570</idno><idno type="pmid">21894570</idno><idno type="doi">10.1007/s10695-011-9541-9</idno><idno type="wicri:Area/PubMed/Corpus">000311</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000311</idno><idno type="wicri:Area/PubMed/Curation">000311</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000311</idno><idno type="wicri:Area/PubMed/Checkpoint">000311</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000311</idno><idno type="wicri:Area/Ncbi/Merge">000399</idno><idno type="wicri:Area/Ncbi/Curation">000399</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Studies on activity, distribution, and zymogram of protease, α-amylase, and lipase in the paddlefish Polyodon spathula.</title><author><name sortKey="Ji, H" sort="Ji, H" uniqKey="Ji H" first="H" last="Ji">H. Ji</name><affiliation wicri:level="1"><nlm:affiliation>College of Animal Science and Technology, Northwest A & F University, Yangling, China. jihong0405@hotmail.com</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Animal Science and Technology, Northwest A & F University, Yangling</wicri:regionArea><wicri:noRegion>Yangling</wicri:noRegion></affiliation></author><author><name sortKey="Sun, H T" sort="Sun, H T" uniqKey="Sun H" first="H T" last="Sun">H T Sun</name></author><author><name sortKey="Xiong, D M" sort="Xiong, D M" uniqKey="Xiong D" first="D M" last="Xiong">D M Xiong</name></author></analytic><series><title level="j">Fish physiology and biochemistry</title><idno type="eISSN">1573-5168</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animal Feed</term><term>Animals</term><term>Carps (metabolism)</term><term>Digestion (physiology)</term><term>Fishes (metabolism)</term><term>Fishes (physiology)</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Lipase (metabolism)</term><term>Peptide Hydrolases (classification)</term><term>Peptide Hydrolases (metabolism)</term><term>Species Specificity</term><term>alpha-Amylases (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lipase</term><term>Peptide Hydrolases</term><term>alpha-Amylases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Carps</term><term>Fishes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Digestion</term><term>Fishes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animal Feed</term><term>Animals</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A series of biochemical determination and electrophoretic observations have been conducted to analyze the activities and characteristics of protease, α-amylase, and lipase of paddlefish Polyodon spathula. The results obtained have been compared with those of bighead carp (Aristichthys nobilis) and hybrid sturgeon (Huso dauricus ♀ × Acipenser schrenki Brandt ♂), in order to increase available knowledge of the physiological characteristics of this sturgeon species and to gain information with regard to its nutrition. Further, a comparative study of enzymatic activity, distribution, and characterization between commercial feed-reared paddlefish (CG) and natural live food-reared (NG) paddlefish was conducted. Results showed that higher proteolytic activity was observed in the pH range 2.5-3.0 and at a pH of 7.0 for paddlefish. Levels of acid protease activity of paddlefish were similar to that of hybrid sturgeon, and significantly higher than that of bighead carp. The inhibition assay of paddlefish showed that the rate of inhibition of tosyl-phenylalanine chloromethyl ketone was approximately 2.6-fold that of tosyl-lysine chloromethyl ketone. There was no significant difference observed for acid protease activity between PG and CG groups, whereas the activity of alkaline protease, α-amylase, and lipase in the PG group were significantly lower than those in the CG group. The substrate sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis further showed that there were certain types of enzymes, especially α-amylase, with similar molecular mass in the paddlefish and hybrid sturgeon. It can be inferred that acid digestion was main mechanism for protein hydrolysis in paddlefish, as reported for other fishes with a stomach. This indicates that the paddlefish requires higher alkaline protease, α-amylase, and lipase activity to digest natural live food.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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