Molecular cloning and characterization of a β-glucanase from Piromyces rhizinflatus

Chu, Chin‐Chou; Tseng, Ching-Yu; Yueh, Pei-Ying; Duan, Chung‐Hang; Liu, Je-Ruei

doi:10.1016/j.jbiosc.2011.01.009

Cited by 9 publications

(3 citation statements)

References 34 publications

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“…3). As recently discussed by Chu et al (2011), a short heating treatment seems to be effective in increasing enzyme activity of some glycoside hydrolases, although the subjacent mechanism is still unknown. Takashima et al (1998) have expressed the same H. grisea cellobiohydrolase gene, which they called exo1, in Aspergillus oryzae.…”

Section: Discussionmentioning

confidence: 98%

An alkaline thermostable recombinant Humicola grisea var. thermoidea cellobiohydrolase presents bifunctional (endo/exoglucanase) activity on cellulosic substrates

Oliveira

Ulhôa

Silveira

et al. 2012

World J Microbiol Biotechnol

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Humicola grisea var. thermoidea is a deuteromycete which secretes a large spectrum of hydrolytic enzymes when grown on lignocellulosic residues. This study focused on the heterologous expression and recombinant enzyme analysis of the major secreted cellulase when the fungus is grown on sugarcane bagasse as the sole carbon source. Cellobiohydrolase 1.2 (CBH 1.2) cDNA was cloned in Pichia pastoris under control of the AOX1 promoter. Recombinant protein (rCBH1.2) was efficiently produced and secreted as a functional enzyme, presenting a molecular mass of 47 kDa. Maximum enzyme production was achieved at 96 h, in culture medium supplemented with 1.34 % urea and 1 % yeast extract and upon induction with 1 % methanol. Recombinant enzyme exhibited optimum activity at 60 °C and pH 8, and presented a remarkable thermostability, particularly at alkaline pH. Activity was evaluated on different cellulosic substrates (carboxymethyl cellulose, filter paper, microcrystalline cellulose and 4-para-nitrophenyl β-D-glucopyranoside). Interestingly, rCBH1.2 presented both exoglucanase and endoglucanase activities and mechanical agitation increased substrate hydrolysis. Results indicate that rCBH1.2 is a potential biocatalyst for applications in the textile industry or detergent formulation.

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Section: Discussionmentioning

confidence: 98%

An alkaline thermostable recombinant Humicola grisea var. thermoidea cellobiohydrolase presents bifunctional (endo/exoglucanase) activity on cellulosic substrates

Oliveira

Ulhôa

Silveira

et al. 2012

World J Microbiol Biotechnol

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“…Ali et al (1995) reported that the molecular weights of xylanase, endoglucanase, and aviselase enzymes, which are members of the cellulase and hemicellulase enzyme family, are in the range of 50kDA to 190kDa.Thanks to its CAZy activities,Piromyces sp. can be used among the microorganisms used in silage production (Wang et al, 2019).Characterization and immobilization studies of the enzyme β-glucosidase, which is involved in the hydrolysis of cellulose, a renewable polysaccharide, have been reported (Chu et al,2011;Tseng et al,2015). 1.4.5.…”

Section: Carbohydrate Active Enzymes System In Neocallimastix Spmentioning

confidence: 99%

Carbohydrate active enzyme system in rumen fungi: a review

YÜCEL

EKİNCİ

2022

International Journal of Secondary Metabolite

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Hydrolysis and dehydration reactions of carbohydrates, which are used as energy raw materials by all living things in nature, are controlled by Carbohydrate Active Enzyme (CAZy) systems. These enzymes are also used in different industrial areas today. There are different types of microorganisms that have the CAZy system and are used in the industrial sector. Apart from current organisms, there are also rumen fungi within the group of candidate microorganisms with the CAZy system. It has been reported that xylanase (EC3.2.1.8 and EC3.2.1.37) enzyme, a member of the glycoside hydrolase enzyme family obtained from Trichoderma sp. and used especially in areas such as bread, paper, and feed industry, is more synthesized in rumen fungi such as Orpinomyces sp. and Neocallimastix sp. Therefore, this study reviews Neocallimastixsp., Orpinomyces sp., Caecomyces sp., Piromyces sp., and Anaeromyces sp., registered in the CAZy and Mycocosm database for rumen fungi to have both CAZy enzyme activity and to be an alternative microorganism in the industry. Furthermore the CAZy enzyme activities of the strains are investigated. The review shows thatNeocallimax sp. and Orpinomyces sp. areconsidered as candidate microorganisms.

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“…Despite the largely reduced set, Salzberg et al conclude by stating: "The more probable explanation for the existence of genes shared by humans and prokaryotes, but missing in nonvertebrates, is a combination of evolutionary rate variation, the small sample of nonvertebrate genomes, and gene biomass [44,45]. In fact, several cellulase genes have been cloned from chytrid fungal strains such as Neocallimastix patriciarum [46], Orpinomyces PC-2 [47], and Piromyces rhizinflatus [48]. More recently, anaerobic gut fungi (and Piromyces sp.…”

Section: Introductionmentioning

confidence: 99%

Contribution of Lateral Gene Transfer to the evolution of the eukaryotic fungus Piromyces sp. E2: Massive bacterial transfer of genes involved in carbohydrate metabolism

Duarte

2019

Preprint

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Lateral gene transfer (also known as Horizontal Gene Transfer) is the transmission of genetic material between phylogenetically unrelated organisms. Previous studies have been showing the importance of this process for the evolution of unicellular eukaryotes, particularly those living in highly competitive niches such as the herbivore gut. Pyromices sp. is an obligate anaerobic chytrid fungus that grows as a commensal organism in the gut of mammalian herbivores, possessing hydrogenosomes instead of mitochondria, producing hydrogen, and playing a key role in the digestion of plant cell wall material. These particular features make its genome particularly valuable for the study of the evolution and adaptation of unicellular eukaryotes to the cellulose-rich and anaerobic environment of the herbivore gut. Here we performed a detailed large-scale lateral gene transfer (LGT) analysis of the genome from the chytrid fungus Piromyces sp. strain E2. For this we set out to elucidate (i) which proteins were likely transferred to its genome, (ii) from which bacterial donor species, and (iii) which functions were laterally acquired. Using sequence comparison and phylogenetic analyses, we have found 704 LGT candidates, representing nearly 5% of the Piromyces sp. orfeome (i.e. the complete set of open reading frames), mostly transferred from Firmicutes, Fibrobacteres, Bacteroidetes and Proteobacteria, closely following the microbial abundance reported for the herbivore gut. With respect to the functional analysis, the LGT candidate set includes proteins from 250 different orthologous groups, with a clear overrepresentation of genes belonging to the Carbohydrate Transport and Metabolism functional class. Finally, we performed a graph density analysis on the metabolic pathways formed by the LGT candidate proteins, showing that the acquired functions fit cohesively within Piromyces metabolic network, and are not randomly distributed within the global KEGG metabolic map. Overall, our study suggests that Piromyces' adaptation to living anaerobically and in the a cellulose-rich environment has been undoubtedly fostered by the acquisition of foreign genes from bacterial neighbors, showing the global importance of such evolutionary mechanisms for successful eukaryotic thriving in such competitive environments. loss in the nonvertebrate lineages." Stanhope et al. (2001) also refute the initial report, arguing that the results are not trustworthy because the method used is not the most appropriate since "phylogenetic reconstruction is critical to synthesizing, from the growing wealth of sequence data, a more comprehensive view of genome evolution." Hence the authors conducted a phylogenetic assessment of 28 proteins (from the 113 corroborated set), discarding all of them as false positives "unlikely to be examples of direct HGT from bacteria to vertebrates." [12] This example clearly shows the controversy surrounding the possibility of lateral gene transfer to multicellular eukaryotes. A more recent publication, in 2015, sets out to resol...

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Molecular cloning and characterization of a β-glucanase from Piromyces rhizinflatus

Cited by 9 publications

References 34 publications

An alkaline thermostable recombinant Humicola grisea var. thermoidea cellobiohydrolase presents bifunctional (endo/exoglucanase) activity on cellulosic substrates

An alkaline thermostable recombinant Humicola grisea var. thermoidea cellobiohydrolase presents bifunctional (endo/exoglucanase) activity on cellulosic substrates

Carbohydrate active enzyme system in rumen fungi: a review

Contribution of Lateral Gene Transfer to the evolution of the eukaryotic fungus Piromyces sp. E2: Massive bacterial transfer of genes involved in carbohydrate metabolism

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