» Articles » PMID: 29484545

Biochemical Properties of α-Amylase from Midgut of Alphitobius Diaperinus (Panzer) (Coleoptera: Tenebrionidae) Larvae

Overview
Journal Neotrop Entomol
Publisher Springer
Specialty Biology
Date 2018 Feb 28
PMID 29484545
Citations 3
Authors
Affiliations
Soon will be listed here.
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 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.

Citing Articles

Insect α-Amylases and Their Application in Pest Management.

Wang B, Huang D, Cao C, Gong Y Molecules. 2023; 28(23).

PMID: 38067617 PMC: 10708458. DOI: 10.3390/molecules28237888.


Proteomics and ultrastructural analysis of Hermetia illucens (Diptera: Stratiomyidae) larval peritrophic matrix.

Lin Y, Rong J, Wei X, Sui Z, Xiao J, Huang D Proteome Sci. 2021; 19(1):7.

PMID: 33836751 PMC: 8035744. DOI: 10.1186/s12953-021-00175-x.


The Amylases of Insects.

Da Lage J Int J Insect Sci. 2018; 10:1179543318804783.

PMID: 30305796 PMC: 6176531. DOI: 10.1177/1179543318804783.

References
1.
Franco O, Rigden D, Melo F, Grossi-de-Sa M . Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases. Eur J Biochem. 2002; 269(2):397-412. DOI: 10.1046/j.0014-2956.2001.02656.x. View

2.
Zheng L, Crippen T, Sheffield C, Poole T, Yu Z, Tomberlin J . Evaluation of Salmonella movement through the gut of the lesser mealworm, Alphitobius diaperinus (Coleoptera: Tenebrionidae). Vector Borne Zoonotic Dis. 2011; 12(4):287-92. DOI: 10.1089/vbz.2011.0613. View

3.
Aggarwal K, Choe L, Lee K . Shotgun proteomics using the iTRAQ isobaric tags. Brief Funct Genomic Proteomic. 2006; 5(2):112-20. DOI: 10.1093/bfgp/ell018. View

4.
Whitehouse C, Dreyer R, Yamashita M, Fenn J . Electrospray interface for liquid chromatographs and mass spectrometers. Anal Chem. 1985; 57(3):675-9. DOI: 10.1021/ac00280a023. View

5.
Ziegler P . Partial purification and characterization of the major endoamylase of mature pea leaves. Plant Physiol. 1988; 86(3):659-66. PMC: 1054548. DOI: 10.1104/pp.86.3.659. View