Cyclodextrin glycosyltransferase encoded by a gene of Paenibacillus azotofixans YUPP-5 exhibited a new function to hydrolyze polysaccharides with β-1,4 linkage

Zhou, Yi; Lee, Yong Seok; Park, Inhye; Sun, Zhengxiang; Yang, Tie; Yang, Pei; Choi, Yong-Lark; Sun, Ming

doi:10.1016/j.enzmictec.2011.12.001

Cited by 11 publications

(7 citation statements)

References 33 publications

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“…The purified PbChi74 in the present study had a molecular mass of 74.6 kDa (Figure 2), which is different from those of chitinases from other Paenibacillus species, including Paenibacillus sp. FPU-7 (61, 78, 82 87, 97, 122, and 153 kDa [11]), P. azotofixans YUPP-5 (70 kDa [21]), and Paenibacillus sp. D1 (56.6 kDa [3]).…”

Section: Discussionmentioning

confidence: 99%

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An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine

Yan

Yang

et al. 2014

Biotechnol Biofuels

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BackgroundN-acetyl-β-D-glucosamine (GlcNAc) is widely used as a valuable pharmacological agent and a functional food additive. The traditional chemical process for GlcNAc production has some problems such as high production cost, low yield, and acidic pollution. Hence, to identify a novel chitinase that is suitable for bioconversion of chitin to GlcNAc is of great value.ResultsA novel chitinase gene (PbChi74) from Paenibacillus barengoltzii was cloned and heterologously expressed in Escherichia coli as an intracellular soluble protein. The gene has an open reading frame (ORF) of 2,163 bp encoding 720 amino acids. The recombinant chitinase (PbChi74) was purified to apparent homogeneity with a purification fold of 2.2 and a recovery yield of 57.9%. The molecular mass of the purified enzyme was estimated to be 74.6 kDa and 74.3 kDa by SDS-PAGE and gel filtration, respectively. PbChi74 displayed an acidic pH optimum of 4.5 and a temperature optimum of 65°C. The enzyme showed high activity toward colloidal chitin, glycol chitin, N-acetyl chitooligosaccharides, and p-nitrophenyl N-acetyl β-glucosaminide. PbChi74 hydrolyzed colloidal chitin to yield N-acetyl chitobiose [(GlcNAc)2] at the initial stage, which was further converted to its monomer N-acetyl glucosamine (GlcNAc), suggesting that it is an exochitinase with β-N-acetylglucosaminidase activity. The purified PbChi74 coupled with RmNAG (β-N-acetylglucosaminidase from Rhizomucor miehei) was used to convert colloidal chitin to GlcNAc, and GlcNAc was the sole end product at a concentration of 27.8 mg mL-1 with a conversion yield of 92.6%. These results suggest that PbChi74 may have great potential in chitin conversion.ConclusionsThe excellent thermostability and hydrolytic properties may give the exochitinase great potential in GlcNAc production from chitin. This is the first report on an exochitinase with N-acetyl-β-D-glucosaminidase activity from Paenibacillus species.

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Section: Discussionmentioning

confidence: 99%

“…[16]. Until now, Paenibacillus species have been reported to produce some endochitinases [3,11-14,18,21], but no exochitinase from Paenibacillus species has been found.…”

Section: Introductionmentioning

confidence: 99%

An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine

Yan

Yang

et al. 2014

Biotechnol Biofuels

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“…fold (Janecȇk, 1997). Most family members hydrolyse α-glucosidic linkages (McCarter & Withers, 1994), except YUPP-5, a CGTase from Paenibacillus azotofixans that can hydrolyse β-1,4-polysaccharide linkages (Zhou et al, 2012). The CGTase contains α-amylase, α-amylase C, TIG, and carbohydrate-binding module (CBM)_20 active sites.…”

Section: Discussionmentioning

confidence: 99%

“…Different lower case letters indicate significant difference at p < .05, t test interest were picked and induced to high-copy number using the CopyControl fosmid autoinduction solution. To screen for the target gene, transformants were inoculated onto the same position of two Petri dishes that contained medium prepared as reported by Zhou et al (2012). After 16 hr at 37 °C, one dish was stained with a 0.2%:2% iodine:KI solution.…”

Section: Discussionmentioning

confidence: 99%

“…Members of this family share a conserved active site architecture and four short conserved sequence regions embedded in a triosephosphate isomerase (TIM) (β/α) 8 structural fold (Janec̆ek, 1997). Most family members hydrolyse α‐glucosidic linkages (McCarter & Withers, 1994), except YUPP‐5, a CGTase from Paenibacillus azotofixans that can hydrolyse β‐1,4‐polysaccharide linkages (Zhou et al, 2012). The CGTase contains α‐amylase, α‐amylase C, TIG, and carbohydrate‐binding module (CBM)_20 active sites.…”

Section: Discussionmentioning

confidence: 99%

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CGTase, a novel antimicrobial protein from Bacillus cereus YUPP‐10, suppresses Verticillium dahliae and mediates plant defence responses

Zhou

Feng

Liu

et al. 2020

Molecular Plant Pathology

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Cotton (Gossypium hirsutum) is one of the most important economic crops and is cultivated in many areas of the world (Ai et al., 2017). Verticillium wilt is a vascular plant disease caused by the soilborne fungus Verticillium dahliae (Fradin & Thomma, 2006; Yadeta & Thomma, 2013; Zhang et al., 2019). The pathogen can adhere to the root surface, and its hyphae penetrate roots to colonize the cortex.

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A β‐mannanase from Paenibacillus sp.: Optimization of production and its possible prebiotic potential

Dhawan¹,

Singh

Kaur

et al. 2015

Biotech and App Biochem

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A thermotolerant bacterium Paenibacillus thiaminolyticus with an ability to produce extracellular β-mannanase was isolated from a soil sample. Bacterium produced 45 U/mL β-mannanase at 50 °C. The culture conditions for high-level production of β-mannanase were optimized. Optimized MS medium [wheat bran 2% (w/v), ammonium sulfate 0.3% (w/v), yeast extract, and peptone (0.025% each) pH 6.5] was inoculated with 2% of 16 H old culture. The culture was incubated at 50 °C for 48 H resulting in 24-folds higher β-mannanase production (1,100 ± 50 U/mL). Optimum pH and temperature for enzyme activity of the crude enzyme was 6.0 and 60 °C, respectively. The enzyme demonstrated 65% relative enzyme activity at 37 °C. The hydrolytic activity of the crude enzymatic preparation was assessed on various agro residues. Thin-layer chromatographic analysis showed that the enzyme activity to saccharify heteromannans resulted in production of a mixture of manno-oligosaccharides (MOS) and enzyme exhibited classic endo-activity. To evaluate the possible prebiotic potential of the MOS thus obtained, initial screening for their ability to support the growth of probiotics was carried out by the pure culture method. Bifidobacterium and Lactobacillus sp. responded positively to the addition of enzymatically derived oligosaccharides and their numbers increased significantly.

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Cyclodextrin glycosyltransferase encoded by a gene of Paenibacillus azotofixans YUPP-5 exhibited a new function to hydrolyze polysaccharides with β-1,4 linkage

Cited by 11 publications

References 33 publications

An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine

An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine

CGTase, a novel antimicrobial protein from Bacillus cereus YUPP‐10, suppresses Verticillium dahliae and mediates plant defence responses

A β‐mannanase from Paenibacillus sp.: Optimization of production and its possible prebiotic potential

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