A novel sucrose hydrolase from the bombycoid silkworms Bombyx mori, Trilocha varians, and Samia cynthia ricini with a substrate specificity for sucrose. (June 2015)
- Record Type:
- Journal Article
- Title:
- A novel sucrose hydrolase from the bombycoid silkworms Bombyx mori, Trilocha varians, and Samia cynthia ricini with a substrate specificity for sucrose. (June 2015)
- Main Title:
- A novel sucrose hydrolase from the bombycoid silkworms Bombyx mori, Trilocha varians, and Samia cynthia ricini with a substrate specificity for sucrose
- Authors:
- Wang, Huabing
Kiuchi, Takashi
Katsuma, Susumu
Shimada, Toru - Abstract:
- Abstract: Although membrane-associated sucrase activity has been detected in the midgut of various lepidopteran species, it has not yet been identified and characterized at the molecular level. In the present study, we identified a novel sucrose hydrolase (SUH) gene from the following three bombycoid silkworms: Bombyx mori, Trilocha varians, and Samia cynthia ricini and named them BmSuh, TvSuh, and ScSuh, respectively. The EST dataset showed that BmSuh is one of the major glycoside hydrolase genes in the larval midgut of B. mori . These genes were almost exclusively expressed in the larval midgut in all three species, mainly at the feeding stage. SUHs are classified into the glycoside hydrolase family 13 and show significant homology to insect maltases. Enzymatic assays revealed that recombinant SUHs were distinct from conventional maltases and exhibited substrate specificity for sucrose. The recombinant BmSUH was less sensitive to sugar-mimic alkaloids than TvSUH and ScSUH, which may explain the reason why the sucrase activity in the B. mori midgut was less affected by the sugar-mimic alkaloids derived from mulberry. Graphical abstract: Highlights: We identified a novel gene encoding sucrose hydrolase (SUH) from each of three bombycoid silkworms. Suh is expressed specifically and abundantly in larval midgut of each species. SUHs show remarkable substrate specificity for sucrose. This property is distinct from other α-glucosidases in insects. Bombyx mori SUH is moreAbstract: Although membrane-associated sucrase activity has been detected in the midgut of various lepidopteran species, it has not yet been identified and characterized at the molecular level. In the present study, we identified a novel sucrose hydrolase (SUH) gene from the following three bombycoid silkworms: Bombyx mori, Trilocha varians, and Samia cynthia ricini and named them BmSuh, TvSuh, and ScSuh, respectively. The EST dataset showed that BmSuh is one of the major glycoside hydrolase genes in the larval midgut of B. mori . These genes were almost exclusively expressed in the larval midgut in all three species, mainly at the feeding stage. SUHs are classified into the glycoside hydrolase family 13 and show significant homology to insect maltases. Enzymatic assays revealed that recombinant SUHs were distinct from conventional maltases and exhibited substrate specificity for sucrose. The recombinant BmSUH was less sensitive to sugar-mimic alkaloids than TvSUH and ScSUH, which may explain the reason why the sucrase activity in the B. mori midgut was less affected by the sugar-mimic alkaloids derived from mulberry. Graphical abstract: Highlights: We identified a novel gene encoding sucrose hydrolase (SUH) from each of three bombycoid silkworms. Suh is expressed specifically and abundantly in larval midgut of each species. SUHs show remarkable substrate specificity for sucrose. This property is distinct from other α-glucosidases in insects. Bombyx mori SUH is more resistant to the sugar-mimic alkaloids in mulberry than those of the other two non-mulberry feeders. … (more)
- Is Part Of:
- Insect biochemistry and molecular biology. Volume 61(2015:Jun.)
- Journal:
- Insect biochemistry and molecular biology
- Issue:
- Volume 61(2015:Jun.)
- Issue Display:
- Volume 61 (2015)
- Year:
- 2015
- Volume:
- 61
- Issue Sort Value:
- 2015-0061-0000-0000
- Page Start:
- 46
- Page End:
- 52
- Publication Date:
- 2015-06
- Subjects:
- Sucrose hydrolase -- Lepidoptera -- Sugar-mimic alkaloids -- Sucrose
Insect biochemistry -- Periodicals
Insects -- Physiology -- Periodicals
Insects -- Molecular aspects -- Periodicals
Biochemistry -- Periodicals
Insectes -- Biochimie -- Périodiques
Insectes -- Composition -- Périodiques
Insectes -- Physiologie -- Périodiques
Insectes -- Aspect moléculaire -- Périodiques
Biochimie -- Périodiques
Biochemistry
Insect biochemistry
Insects -- Molecular aspects
Insects -- Physiology
Periodicals
572.8157 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09651748 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.ibmb.2015.04.005 ↗
- Languages:
- English
- ISSNs:
- 0965-1748
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4516.852000
British Library DSC - BLDSS-3PM
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