Purification and characterization of a new thermoalkaliphilic pectate lyase from Actinomadura keratinilytica Cpt20

Saoudi, Boudjema; Habbeche, Amina; Kerouaz, Bilal; Haberra, Soumaya; Romdhane, Zamen Ben; Tichati, Lazhari; Boudelaa, Mokhtar; Belghith, Hafedh; Gargouri, Ali; Ladjama, Ali

doi:10.1016/j.procbio.2015.10.006

Cited by 14 publications

(12 citation statements)

References 44 publications

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“…BspPel showed higher activity than many enzymes such as PEL68P ( Zhang et al, 2013 ), PL ( Zhuge et al, 2008 ), Pectate lyase ( Chiliveri and Linga, 2014 ), BsPel-PB1 ( Zhou et al, 2017c ), and PpPel10a ( Zhao et al, 2018 ) when treated at 70°C. To our best knowledge, only Pel-20 ( Saoudi et al, 2015 ) and Pel SWU ( Sukhumsiirchart et al, 2009 ) retained more activity than BspPel at 70°C, but BspPel was treated with a higher pH, which had important effects on activity. The residual activity of BspPel was reduced to approximately 19% and 7% after incubation at 60°C and 70°C for 4 h, respectively.…”

Section: Resultsmentioning

confidence: 87%

High-Level Expression and Biochemical Properties of A Thermo-Alkaline Pectate Lyase From Bacillus sp. RN1 in Pichia pastoris With Potential in Ramie Degumming

Zheng

Zhang

Liu

et al. 2020

Front. Bioeng. Biotechnol.

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Pectate lyases play an essential role in textiles, animal feed, and oil extraction industries. Pichia pastoris can be an ideal platform for pectate lyases production, and BspPel (a thermo-alkaline pectate lyase from Bacillus sp. RN1) was overexpressed by combined strategies, reaching 1859 U/mL in a 50 L fermentator. It displayed the highest activity at 80 • C, and maintained more than 60% of the activity between 30 and 70 • C for 1 h. It showed an optimal pH of 10.0, and exhibited remarkable stability over a wider pH range (3.0-11.0), retaining more than 80.0% of enzyme activity for 4 h. The K m and k cat of BspPel on PGA (polygalacturonic acid) was 2.19 g L −1 and 116.1 s −1 , respectively. The activity was significantly enhanced by Ca 2+ , Mn 2+ , and Cu 2+ , and a slight increase was observed with the addition of Ba 2+ and Mg 2+. Scanning electron microscope was used to show the degumming efficiency of BspPel on ramie fibers. The loss weight was 9.2% when treated with crude enzyme supernatant and 20.8% when treated with the enzyme-chemical method, which was higher than the 14.2% weight loss in the positive control treated with 0.5% (w/v) NaOH alone. In conclusion, BspPel could be a good candidate for the ramie degumming industry.

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Section: Resultsmentioning

confidence: 87%

High-Level Expression and Biochemical Properties of A Thermo-Alkaline Pectate Lyase From Bacillus sp. RN1 in Pichia pastoris With Potential in Ramie Degumming

Zheng

Zhang

Liu

et al. 2020

Front. Bioeng. Biotechnol.

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“…In the process of mutual recognition of plant hosts and pathogens, pathogenic fungi can secrete cell wall-degrading enzymes (CWDEs), mainly including cellulase, pectinase, cutinase, and so on. Cellulase, pectinase, and cutinase play an important role in anthracnose. , Therefore, CWDEs are important components of plant pathogenic fungi. , Pectate lyase (PL) is common in plant pathogenic bacteria, fungi, and nematodes; moreover, it is an important pathogenic factor that degrades the host cell wall and increases the susceptibility of plants to pathogens . The important genes associated with PL coding, plyD (CGGC5_1824), plyE (CGGC5_11629), and plyF (CGGC5_13439) were found to be downregulated in both analyses (Table , spot 32–34).…”

Section: Discussionmentioning

confidence: 99%

Antifungal Mechanism of Volatile Organic Compounds Produced by Bacillus subtilis CF-3 on Colletotrichum gloeosporioides Assessed Using Omics Technology

Wang

Qin

et al. 2021

J. Agric. Food Chem.

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Bacillus subtilis is commonly used as a biocontrol bacterium owing to its strong antifungal activity, broad-spectrum inhibition, and general safety. In this study, the inhibitory effects of volatile organic compounds (VOCs) produced by B. subtilis CF-3 on Colletotrichum gloeosporioides, a major destructive phytopathogen of litchi anthracnose, were analyzed using proteomics and transcriptomics. Differentially expressed genes (DEGs) and proteins (DEPs) indicated that the inhibition of C. gloeosporioides by B. subtilis CF-3 VOCs downregulated the expression of genes related to cell membrane fluidity, cell wall integrity, energy metabolism, and production of cell wall-degrading enzymes. Particularly, those important DEGs and DEPs related to the ergosterol biosynthetic and biosynthesis of unsaturated fatty acids are most significantly influenced. 2,4-di-tert-butylphenol, a characteristic component of B. subtilis CF-3 VOCs, also showed a similar effect on C. gloeosporioides. Our results provide a theoretical basis for the potential application of B. subtilis CF-3 in the postharvest protection of fruits and vegetables.

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“…1B and 1C), gradually decreased with the increasing age of the wild Asian elephants. The above microflorae were closely related to the digestion of lignocellulose [3,[31][32][33][34][35][36]. The gradually change in abundance of these microflorae might give hints for the subsequent study of the ability of wild Asian elephants to digest lignocellulose as they grow.…”

Section: Microbial Diversity In the Fecal Metagenomes Of The Three Asian Elephantsmentioning

confidence: 95%

Metagenomic Analysis of the Fecal Microbiomes of Wild Asian Elephants Reveals Microflora and Enzymes that Mainly Digest Hemicellulose

Zhang¹,

Xu²,

Huang³

et al. 2019

Journal of Microbiology and Biotechnology

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To investigate the diversity of gastrointestinal microflora and lignocellulose-degrading enzymes in wild Asian elephants, three of these animals living in the same group were selected for study from the Wild Elephant Valley in the Xishuangbanna Nature Reserve of Yunnan Province, China. Fresh fecal samples from the three wild Asian elephants were analyzed by metagenomic sequencing to study the diversity of their gastrointestinal microbes and cellulolytic enzymes. There were a high abundance of Firmicutes and a higher abundance of hemicellulose-degrading hydrolases than cellulose-degrading hydrolases in the wild Asian elephants. Furthermore, there were a high abundance and a rich diversity of carbohydrate active enzymes (CAZymes) obtained from the gene set annotation of the three samples, with the majority of them showing low identity with the CAZy database entry. About half of the CAZymes had no species source at the phylum or genus level. These indicated that the wild Asian elephants might possess greater ability to digest hemicellulose than cellulose to provide energy, and moreover, the gastrointestinal tracts of these pachyderms might be a potential source of novel efficient lignocellulose-degrading enzymes. Therefore, the exploitation and utilization of these enzyme resources could help us to alleviate the current energy crisis and ensure food security.

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Purification and characterization of a new thermoalkaliphilic pectate lyase from Actinomadura keratinilytica Cpt20

Cited by 14 publications

References 44 publications

High-Level Expression and Biochemical Properties of A Thermo-Alkaline Pectate Lyase From Bacillus sp. RN1 in Pichia pastoris With Potential in Ramie Degumming

High-Level Expression and Biochemical Properties of A Thermo-Alkaline Pectate Lyase From Bacillus sp. RN1 in Pichia pastoris With Potential in Ramie Degumming

Antifungal Mechanism of Volatile Organic Compounds Produced by Bacillus subtilis CF-3 on Colletotrichum gloeosporioides Assessed Using Omics Technology

Metagenomic Analysis of the Fecal Microbiomes of Wild Asian Elephants Reveals Microflora and Enzymes that Mainly Digest Hemicellulose

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