Biochemical Properties of α-Amylase from Midgut of Alphitobius diaperinus (Panzer) (Coleoptera: Tenebrionidae) Larvae
The lesser mealworm, Alphitobius diaperinus (Panzer), is the main insect pest in the poultry industry, thus causing serious damage to production. In this work, the properties of midgut α-amylase from larvae of A . diaperinus were characterized, and its in vitro activity to proteinaceous preparations...
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| Veröffentlicht in: | Neotropical entomology 2018-10, Vol.47 (5), p.698-708 |
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| creator | Cruz, W O Sinhori, G G C de Lima, C A R Pontes, E G |
| description | The lesser mealworm,
Alphitobius diaperinus
(Panzer), is the main insect pest in the poultry industry, thus causing serious damage to production. In this work, the properties of midgut α-amylase from larvae of
A
.
diaperinus
were characterized, and its in vitro activity to proteinaceous preparations from different cultivars of common bean (
Phaseolus vulgaris
) was determined, as well as the amylolitic activity of insects reared on different types of poultry diet. In order to establish some assay conditions, time course and enzyme concentration upon the reaction rate were determined. Product proceeded linearly with time, and the activity was directly proportional to the enzyme concentration. Banding patterns in mildly denaturing electrophoresis showed a single band with apparent molecular weight of 42 kDa. α-Amylase reached optimal temperature at 45°C and pH 5.0 as the optimal one. It maintained 34.6% of the activity after being kept at 60°C for 5 min, and 23%, after 60 min. However, at 80°C, only 14 and 6% remained after 5 and 60 min, respectively. The presence of Ca
2+
and Na
+
ions decreased the enzyme activity at concentrations higher than 2 and 100 mM, respectively. The activity was significantly inhibited by some proteinaceous extracts from common bean cultivars, and it declined with increasing proteinaceous concentration. No significant difference was observed when the amylolytic activity was determined in
A
.
diaperinus
reared on different poultry diets, offered to broilers in the starter, grower, finisher, and layer phases. |
| doi_str_mv | 10.1007/s13744-018-0590-y |
| format | Article |
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Alphitobius diaperinus
(Panzer), is the main insect pest in the poultry industry, thus causing serious damage to production. In this work, the properties of midgut α-amylase from larvae of
A
.
diaperinus
were characterized, and its in vitro activity to proteinaceous preparations from different cultivars of common bean (
Phaseolus vulgaris
) was determined, as well as the amylolitic activity of insects reared on different types of poultry diet. In order to establish some assay conditions, time course and enzyme concentration upon the reaction rate were determined. Product proceeded linearly with time, and the activity was directly proportional to the enzyme concentration. Banding patterns in mildly denaturing electrophoresis showed a single band with apparent molecular weight of 42 kDa. α-Amylase reached optimal temperature at 45°C and pH 5.0 as the optimal one. It maintained 34.6% of the activity after being kept at 60°C for 5 min, and 23%, after 60 min. However, at 80°C, only 14 and 6% remained after 5 and 60 min, respectively. The presence of Ca
2+
and Na
+
ions decreased the enzyme activity at concentrations higher than 2 and 100 mM, respectively. The activity was significantly inhibited by some proteinaceous extracts from common bean cultivars, and it declined with increasing proteinaceous concentration. No significant difference was observed when the amylolytic activity was determined in
A
.
diaperinus
reared on different poultry diets, offered to broilers in the starter, grower, finisher, and layer phases.</description><identifier>ISSN: 1519-566X</identifier><identifier>EISSN: 1678-8052</identifier><identifier>DOI: 10.1007/s13744-018-0590-y</identifier><identifier>PMID: 29484545</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Agriculture ; alpha-Amylases - antagonists & inhibitors ; alpha-Amylases - chemistry ; Animal Feed - parasitology ; Animals ; Biomedical and Life Sciences ; Coleoptera - enzymology ; Digestive System - enzymology ; Entomology ; Enzyme Inhibitors - chemistry ; Enzyme Stability ; Larva - enzymology ; Life Sciences ; Pest Management ; Phaseolus - chemistry ; Poultry</subject><ispartof>Neotropical entomology, 2018-10, Vol.47 (5), p.698-708</ispartof><rights>Sociedade Entomológica do Brasil 2018</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c344t-46f5f0b65360593ae824a3e1d1c9fa2bb39079f2a365a5075ff5d0e7521680333</citedby><cites>FETCH-LOGICAL-c344t-46f5f0b65360593ae824a3e1d1c9fa2bb39079f2a365a5075ff5d0e7521680333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13744-018-0590-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13744-018-0590-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27911,27912,41475,42544,51306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29484545$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cruz, W O</creatorcontrib><creatorcontrib>Sinhori, G G C</creatorcontrib><creatorcontrib>de Lima, C A R</creatorcontrib><creatorcontrib>Pontes, E G</creatorcontrib><title>Biochemical Properties of α-Amylase from Midgut of Alphitobius diaperinus (Panzer) (Coleoptera: Tenebrionidae) Larvae</title><title>Neotropical entomology</title><addtitle>Neotrop Entomol</addtitle><addtitle>Neotrop Entomol</addtitle><description>The lesser mealworm,
Alphitobius diaperinus
(Panzer), is the main insect pest in the poultry industry, thus causing serious damage to production. In this work, the properties of midgut α-amylase from larvae of
A
.
diaperinus
were characterized, and its in vitro activity to proteinaceous preparations from different cultivars of common bean (
Phaseolus vulgaris
) was determined, as well as the amylolitic activity of insects reared on different types of poultry diet. In order to establish some assay conditions, time course and enzyme concentration upon the reaction rate were determined. Product proceeded linearly with time, and the activity was directly proportional to the enzyme concentration. Banding patterns in mildly denaturing electrophoresis showed a single band with apparent molecular weight of 42 kDa. α-Amylase reached optimal temperature at 45°C and pH 5.0 as the optimal one. It maintained 34.6% of the activity after being kept at 60°C for 5 min, and 23%, after 60 min. However, at 80°C, only 14 and 6% remained after 5 and 60 min, respectively. The presence of Ca
2+
and Na
+
ions decreased the enzyme activity at concentrations higher than 2 and 100 mM, respectively. The activity was significantly inhibited by some proteinaceous extracts from common bean cultivars, and it declined with increasing proteinaceous concentration. No significant difference was observed when the amylolytic activity was determined in
A
.
diaperinus
reared on different poultry diets, offered to broilers in the starter, grower, finisher, and layer phases.</description><subject>Agriculture</subject><subject>alpha-Amylases - antagonists & inhibitors</subject><subject>alpha-Amylases - chemistry</subject><subject>Animal Feed - parasitology</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Coleoptera - enzymology</subject><subject>Digestive System - enzymology</subject><subject>Entomology</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Stability</subject><subject>Larva - enzymology</subject><subject>Life Sciences</subject><subject>Pest Management</subject><subject>Phaseolus - chemistry</subject><subject>Poultry</subject><issn>1519-566X</issn><issn>1678-8052</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1u1DAUhS0EoqXwAGyQl9OF4fovcdgNI_6kQXRRJHaWk1y3rpI42Eml4a14EZ4Jj6awZHWPdM850vkIecnhNQeo32Qua6UYcMNAN8AOj8g5r2rDDGjxuGjNG6ar6vsZeZbzHYCoZaWfkjPRKKO00ufk_l2I3S2OoXMDvUpxxrQEzDR6-vsX246HwWWkPsWRfgn9zbocP9thvg1LbMOaaR9cyYSpyM2Vm35iuqSbXRwwzgsm95Ze44RtCnEKvcNLunfp3uFz8sS7IeOLh3tBvn14f737xPZfP37ebfesk0otTFVee2grLasyUDo0QjmJvOdd451oW9lA3Xjhyiynodbe6x6w1oJXBqSUF2Rz6p1T_LFiXuwYcofD4CaMa7YCwJgGjBbFyk_WLsWcE3o7pzC6dLAc7BG3PeG2Bbc94raHknn1UL-2I_b_En_5FoM4GXJ5TTeY7F1c01Qm_6f1D3uwjEE</recordid><startdate>20181001</startdate><enddate>20181001</enddate><creator>Cruz, W O</creator><creator>Sinhori, G G C</creator><creator>de Lima, C A R</creator><creator>Pontes, E G</creator><general>Springer US</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20181001</creationdate><title>Biochemical Properties of α-Amylase from Midgut of Alphitobius diaperinus (Panzer) (Coleoptera: Tenebrionidae) Larvae</title><author>Cruz, W O ; Sinhori, G G C ; de Lima, C A R ; Pontes, E G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c344t-46f5f0b65360593ae824a3e1d1c9fa2bb39079f2a365a5075ff5d0e7521680333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Agriculture</topic><topic>alpha-Amylases - antagonists & inhibitors</topic><topic>alpha-Amylases - chemistry</topic><topic>Animal Feed - parasitology</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Coleoptera - enzymology</topic><topic>Digestive System - enzymology</topic><topic>Entomology</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Stability</topic><topic>Larva - enzymology</topic><topic>Life Sciences</topic><topic>Pest Management</topic><topic>Phaseolus - chemistry</topic><topic>Poultry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cruz, W O</creatorcontrib><creatorcontrib>Sinhori, G G C</creatorcontrib><creatorcontrib>de Lima, C A R</creatorcontrib><creatorcontrib>Pontes, E G</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Neotropical entomology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cruz, W O</au><au>Sinhori, G G C</au><au>de Lima, C A R</au><au>Pontes, E G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical Properties of α-Amylase from Midgut of Alphitobius diaperinus (Panzer) (Coleoptera: Tenebrionidae) Larvae</atitle><jtitle>Neotropical entomology</jtitle><stitle>Neotrop Entomol</stitle><addtitle>Neotrop Entomol</addtitle><date>2018-10-01</date><risdate>2018</risdate><volume>47</volume><issue>5</issue><spage>698</spage><epage>708</epage><pages>698-708</pages><issn>1519-566X</issn><eissn>1678-8052</eissn><abstract>The lesser mealworm,
Alphitobius diaperinus
(Panzer), is the main insect pest in the poultry industry, thus causing serious damage to production. In this work, the properties of midgut α-amylase from larvae of
A
.
diaperinus
were characterized, and its in vitro activity to proteinaceous preparations from different cultivars of common bean (
Phaseolus vulgaris
) was determined, as well as the amylolitic activity of insects reared on different types of poultry diet. In order to establish some assay conditions, time course and enzyme concentration upon the reaction rate were determined. Product proceeded linearly with time, and the activity was directly proportional to the enzyme concentration. Banding patterns in mildly denaturing electrophoresis showed a single band with apparent molecular weight of 42 kDa. α-Amylase reached optimal temperature at 45°C and pH 5.0 as the optimal one. It maintained 34.6% of the activity after being kept at 60°C for 5 min, and 23%, after 60 min. However, at 80°C, only 14 and 6% remained after 5 and 60 min, respectively. The presence of Ca
2+
and Na
+
ions decreased the enzyme activity at concentrations higher than 2 and 100 mM, respectively. The activity was significantly inhibited by some proteinaceous extracts from common bean cultivars, and it declined with increasing proteinaceous concentration. No significant difference was observed when the amylolytic activity was determined in
A
.
diaperinus
reared on different poultry diets, offered to broilers in the starter, grower, finisher, and layer phases.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>29484545</pmid><doi>10.1007/s13744-018-0590-y</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Neotropical entomology, 2018-10, Vol.47 (5), p.698-708 |
| issn | 1519-566X 1678-8052 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Agriculture alpha-Amylases - antagonists & inhibitors alpha-Amylases - chemistry Animal Feed - parasitology Animals Biomedical and Life Sciences Coleoptera - enzymology Digestive System - enzymology Entomology Enzyme Inhibitors - chemistry Enzyme Stability Larva - enzymology Life Sciences Pest Management Phaseolus - chemistry Poultry |
| title | Biochemical Properties of α-Amylase from Midgut of Alphitobius diaperinus (Panzer) (Coleoptera: Tenebrionidae) Larvae |
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