Comparative Characterization of Chitinases from Silkworm (Bombyx mori) and Bollworm (Helicoverpa armigera)

Zhang, Hongbin; Liu, Mingyan; Tian, Yangchao; Hu, Xueqin

doi:10.1007/s12013-011-9196-2

Cited by 17 publications

(11 citation statements)

References 28 publications

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“…Chitinases of insects are degrading enzymes that function during ecdysis (Zhang et al 2011). These are primarily endochitinases that randomly cleave chitin present in the cuticle to chitooligosaccharides that are further hydrolyzed by exoenzymes to N-acetyl-glucosamine monomer, which is reused to synthesize a new cuticle (Chaudhari et al 2013).…”

Section: Chitinase Sourcesmentioning

confidence: 99%

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

et al. 2015

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Chitinases are ubiquitous class of extracellular enzymes, which have gained attention in the past few years due to their wide biotechnological applications. The effectiveness of conventional insecticides is increasingly compromised by the occurrence of resistance; thus, chitinase offers a potential alternative to the use of chemical fungicides. The thermostable enzymes from thermophilic microorganisms have numerous industrial, medical, environmental and biotechnological applications due to their high stability for temperature and pH. Thermomyces lanuginosus produced a large number of chitinases, of which chitinase I and II are successfully cloned and purified recently. Molecular dynamic simulations revealed that the stability of these enzymes are maintained even at higher temperature. In this review article we have focused on chitinases from different sources, mainly fungal chitinase of T. lanuginosus and its industrial application.

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Section: Chitinase Sourcesmentioning

confidence: 99%

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

et al. 2015

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“…Solid chitin powder was purchased from TCI (Tokyo, Japan). Colloidal chitin was prepared from solid chitin according to the instructions described by Zhang et al (2011). Chitosan (70 and 100% deacetylated) was kindly gifted by Prof. Subbaratnam Muthukrishnan from Kansas State University.…”

Section: Chitin Binding Assaysmentioning

confidence: 99%

Studies on the chitin/chitosan binding properties of six cuticular proteins analogous to peritrophin 3 from Bombyx mori

Ren

Liu

et al. 2017

Insect Molecular Biology

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Chitin deacetylation is required to make the cuticle rigid and compact through chitin chain crosslinking. Thus it is presumed that specialized proteins are required to bind deacetylated chitin chains together. However, deacetylated-chitin binding proteins have not ever been reported. In a previous work, six cuticular proteins analogous to peritrophin 3 (CPAP3s) were found to be abundant in the moulting fluid of Bombyx mori. In this study, these BmCPAP3s (BmCPAP3-A1, BmCPAP3-A2, BmCPAP3-B, BmCPAP3-C, BmCPAP3-D1 and BmCPAP3-D2) were cloned and expressed in Escherichia coli and purified using metal-chelating affinity chromatography. Their binding activities demonstrated that although all of the BmCPAP3s showed similar binding abilities toward crystalline chitin and colloidal chitin, they differed in their affinities toward partially and fully deacetylated chitin. Amongst them, BmCPAP3-D1 exhibited the highest binding activity toward deacetylated chitin. The gene expression pattern of BmCPAP3-D1 was similar to BmCPAP3-A1 and BmCPAP3-C at most stages except that it was dramatically upregulated at the beginning of the pupa to adult transition stage. This work is the first report of a chitin-binding protein, BmCPAP3-D1, which exhibits high binding affinity to deacetylated chitin.

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“…, α-chitin (TCI, Tokyo, Japan) or colloidal chitin (prepared according to the instructions described by Zhang et al, 2011a) was used as substrate to determine chitinase activity. When pNP-β-(GlcNAc) 2 was used as substrate, the reaction mixture (60 μL) consisted of pNP-β-(GlcNAc) 2 , an appropriate amount of enzyme and Britton-Robinson's wide range buffer.…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…Insect chitinases play vital roles during molting and metamorphosis. To date, insect chitinases have been obtained from different insects, including dipterans (Yan et al , 2002; Zhang et al , 2011b; Ramalho‐Ortigao & Traub‐Cseko, 2003; Zhang et al , 2011c; Filho et al , 2002; Zhu et al , 2008b; Zhu et al , 2008a), lepidopterans (Kimura, 1976; Zheng et al , 2002; Shinoda et al , 2001; Fitches et al , 2004; Lu et al , 2002), coleopterans (Genta et al , 2006; Zhu et al , 2008c; Zhu et al , 2008a; Royer et al , 2002; Zhu et al , 2008b), hymenopterans (Krishnan et al , 1994; Erthal et al , 2007) and hemipterans (Nakabachi et al , 2010). Based on amino acid sequence similarity, insect chitinases and chitinase‐like proteins can be classified into eight groups (Arakane & Muthukrishnan, 2010; Zhang et al , 2011b).…”

Section: Introductionmentioning

confidence: 99%

Cloning, expression and biocharacterization of OfCht5, the chitinase from the insect Ostrinia furnacalis

Liu

Yang

2012

Insect Science

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Chitinase catalyzes β-1,4-glycosidic linkages in chitin and has attracted research interest due to it being a potential pesticide target and an enzymatic tool for preparation of N-acetyl-β-D-glucosamine. An individual insect contains multiple genes encoding chitinases, which vary in domain architectures, expression patterns, physiological roles and biochemical properties. Herein, OfCht5, the glycoside hydrolase family 18 chitinase from the widespread lepidopteran pest Ostrinia furnacalis, was cloned, expressed in the yeast Pichia pastoris and biochemically characterized in an attempt to facilitate both pest control and biomaterial preparation. Complementary DNA sequence analysis indicated that OfCHT5 consisted of an open reading frame of 1 665-bp nucleotides. Phylogenic analysis suggested OfCht5 belongs to the Group I insect chitinases. Expression of OfCht5 in Pichia pastoris resulted in highest specific activity after 120 h of induction with methanol. Through two steps of purification, consisting of ammonium sulfate precipitation and metal chelating chromatography, about 7 mg of the recombinant OfCht5 was purified to homogeneity from 1 L culture supernatant. OfCht5 effectively converted colloidal chitin into chitobiose, but had relatively low activity toward α-chitin. When chitooligosaccharides [(GlcNAc)n , n= 3-6] were used as substrates, OfCht5 was observed to possess the highest catalytic efficiency parameter toward (GlcNAc)4 and predominantely hydrolyzed the second glycosidic bond from the non-reducing end. Together with β-N-acetyl-D-hexosaminidase OfHex1, OfCht5 achieved its highest efficiency in chitin degradation that yielded N-acetyl-β-D-glucosamine, a valuable pharmacological reagent and food supplement, within a molar concentration ratio of OfCht5 versus OfHex1 in the range of 9 : 1-15 : 1. This work provides an alternative to existing preparation of chitinase for pesticides and other applications.

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Comparative Characterization of Chitinases from Silkworm (Bombyx mori) and Bollworm (Helicoverpa armigera)

Cited by 17 publications

References 28 publications

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

Studies on the chitin/chitosan binding properties of six cuticular proteins analogous to peritrophin 3 from Bombyx mori

Cloning, expression and biocharacterization of OfCht5, the chitinase from the insect Ostrinia furnacalis

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