Cloning and expression of a novel α-1,3-arabinofuranosidase from Penicillium oxalicum sp. 68

Hu, Yanbo; Yan, Xuecui; Zhang, Han; Liu, Jiaqi; Luo, Feng; Cui, Yingying; Wang, Weiyang; Zhou, Yifa

doi:10.1186/s13568-018-0577-4

Cited by 16 publications

(9 citation statements)

References 46 publications

(46 reference statements)

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“…3). Activity on pectin-related arabinan has also been reported for related enzymes, such as Abf62A from Penicillium oxalicum [33] and Abf62A and Abf62C from Mycothermus thermophilus [34]. It has been suggested that this activity is particularly related to the a-1,3-L-arabinose decorations of the a-1,5-L-arabinose backbone or arabinan [32].…”

Section: P Subrubescens Abfs Display Highly Diverse Activities On Nat...mentioning

confidence: 81%

Comparative characterization of nine novel GH51, GH54 and GH62 α‐l‐arabinofuranosidases from Penicillium subrubescens

Linares

Dilokpimol

2022

FEBS Letters

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Edited by Ulf-Ingo Fl€ ugge a-L-Arabinofuranosidases (ABFs) are important enzymes in plant biomass degradation with a wide range of applications. The ascomycete fungus Penicillium subrubescens has more a-L-arabinofuranosidase-encoding genes in its genome compared to other Penicillia. We characterized nine ABFs from glycoside hydrolase (GH) families GH51, GH54 and GH62 from this fungus and demonstrated that they have highly diverse specificity and activity levels, indicating that the expansion was accompanied by diversification of the enzymes. Comparison of the substrate preference of the enzymes to the expression of the corresponding genes when the fungus was grown on either of two plant biomass substrates did not show a clear correlation, suggesting a more complex regulatory system governing L-arabinose release from plant biomass by P. subrubescens.

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Section: P Subrubescens Abfs Display Highly Diverse Activities On Nat...mentioning

confidence: 81%

Comparative characterization of nine novel GH51, GH54 and GH62 α‐l‐arabinofuranosidases from Penicillium subrubescens

Linares

Dilokpimol

2022

FEBS Letters

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“…39 P. oxalicum is applied in the industrial production of glycoside hydrolase. 40 A study suggests that this species has potential applications in βxylosidase production. 41 E. amstelodami (57.1% frequency of occurrence), which is widely found in Fuzhuan brick tea and Pu'er tea, is believed to be one of the spices that form the "golden flower" in dark tea.…”

Section: ■ Discussionmentioning

confidence: 99%

Evaluation of Mycoflora and Citrinin Occurrence in Chinese Liupao Tea

Mao

Teng

et al. 2020

J. Agric. Food Chem.

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Citrinin (CIT), a known nephrotoxic mycotoxin, is mainly produced by Penicillium, Aspergillus, and Monascus species. It is a natural contaminant in cereal grains, foods, and feedstuff. Liupao tea (or Liubao tea) is a typical Chinese dark tea obtained via indigenous tea fermentation facilitated by microorganisms. Certain fungi present in Liupao tea that may produce CIT are a potential threat to consumer health. In the present study, various potential toxigenic mycoflora and the natural occurrence of CIT in Liupao tea were surveyed via the culture-dependent method, high performance liquid chromatography−fluorescence detection (HPLC− FLD), and ultrahigh performance liquid chromatography−tandem mass spectrometry (UHPLC−MS/MS). Total mold counts ranged from 3.5 × 10 2 CFU/g to 2.1 × 10 6 CFU/g tea in 28 tea samples. A total of 218 fungal isolates belonging to five genera and 23 species were identified. Some of these strains, such as Aspergillus ochraceus, Aspergillus oryzae, Penicillium citrinum, and Penicillium chrysogenum, may potentially be a CIT-producing species. In addition, 32.7% of 113 Liupao tea samples were contaminated with CIT at concentrations ranging from 7.8 to 206.1 μg/kg. These CIT concentrations in Liupao tea are chiefly attributed to climatic conditions and water activity during storage that favor fungal proliferation and mycotoxin production. However, CIT could not be detected in Liupao tea stored for over 10 years. These results provide the first information about the potential toxigenic mycoflora and natural occurrence of CIT in Liupao tea. Therefore, storage conditions and fungal community must be monitored to ensure the quality of Liupao tea.

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“…Strain P. oxalicum sp. 68 was isolated from soil in Changbai Mountain (Jilin Province, China), and stored in China General Microbiological Culture Collection Center (collection number CGMCC 7.328) [ 27 ]. P. pastoris GS115 and p PICZα A (Novagen, USA) were used as host and expression vectors, respectively.…”

Section: Methodsmentioning

confidence: 99%

Molecular Cloning and Characterization of a Novel Exo-β-1,3-Galactanase from Penicillium oxalicum sp. 68

Zhou

Yan

et al. 2022

J. Microbiol. Biotechnol.

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β-D-(1→4)-galactan, whereas AG-II is β-D-(1→3) and/or (1→6)-galactan. Large quantities of AGs are present in Larix trees [1][2][3], and have been shown to possess diverse biological properties, including immunological activity [4], antitumor [5], and antiviral effects [6]. AGs from Larix laricina have been reported to play a unique role in reducing the incidence of the common cold [7]. In addition, AGs have been approved by the US Food and Drug Administration (FDA) for use as dietary fiber. AG-mediated biological activity is generally associated with its monosaccharide composition, type of glycosidic linkage, molecular weight, as well as the number and type of substituents and branched chains. Therefore, analysis of the complex fine structure and function is a significant problem in glycobiology.Glycoside hydrolase is an important enzyme that is widely used in the study of polysaccharides [8]. Up to now, about 171 glycoside hydrolase families have been reported in the CAZy database [9]. β-Galactanases are a broad group of enzymes that hydrolyze glycosidic bonds in plant-derived galactans, and have been widely used in the analysis of polysaccharide structures, construction of medicinal plant fingerprints, preparation of galactooligosaccharides, and food quality improvement [10][11][12]. This group of enzymes can be divided into β-1,3-galactanase, β-1,4galactanase and β-1,6-galactanase according to the structure of their substrates [13]. At present, there are many studies on the preparation and functional analysis of β-1,4-galactanase, whereas investigations with β-1,3-and β-1,6-galactanases are relatively rare [14,15]. Therefore, it has become crucial to the field to prepare and characterize β-1,3-and β-1,6-galactanases. Arabinogalactans have diverse biological properties and can be used as pharmaceutical agents.Most arabinogalactans are composed of β-(1 → 3)-galactan, so it is particularly important to identify β-1,3-galactanases that can selectively degrade them. In this study, a novel exo-β-1,3-galactanase, named PoGal3, was screened from Penicillium oxalicum sp. 68, and hetero-expressed in P. pastoris GS115 as a soluble protein. PoGal3 belongs to glycoside hydrolase family 43 (GH43) and has a 1,356bp gene length that encodes 451 amino acids residues. To study the enzymatic properties and substrate selectivity of PoGal3, β-1,3-galactan (AG-P-I) from larch wood arabinogalactan (LWAG) was prepared and characterized by HPLC and NMR. Using AG-P-I as substrate, purified PoGal3 exhibited an optimal pH of 5.0 and temperature of 40°C. We also discovered that Zn 2+ had the strongest promoting effect on enzyme activity, increasing it by 28.6%. Substrate specificity suggests that PoGal3 functions as an exo-β-1,3-galactanase, with its greatest catalytic activity observed on AG-P-I. Hydrolytic products of AG-P-I are mainly composed of galactose and β-1,6-galactobiose. In addition, PoGal3 can catalyze hydrolysis of LWAG to produce galacto-oligomers. PoGal3 is the first enzyme identified as an exo-β-1,3-galactanase that can b...

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Cloning and expression of a novel α-1,3-arabinofuranosidase from Penicillium oxalicum sp. 68

Cited by 16 publications

References 46 publications

Comparative characterization of nine novel GH51, GH54 and GH62 α‐l‐arabinofuranosidases from Penicillium subrubescens

Comparative characterization of nine novel GH51, GH54 and GH62 α‐l‐arabinofuranosidases from Penicillium subrubescens

Evaluation of Mycoflora and Citrinin Occurrence in Chinese Liupao Tea

Molecular Cloning and Characterization of a Novel Exo-β-1,3-Galactanase from Penicillium oxalicum sp. 68

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