Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: Phylogenetic analysis of ErPelPL1 with other pectate lyases of PL1 family. Different color blocks correspond to subfamilies of PL1 family, respectively

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques:

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: Multiple sequences alignment of ErPelPL1 and partial pectate lyases from the PL1 family. Namely, PelC ( Erwinia chrysanthemii EC16, AAA24849.1), Pel ( Rhodopirellula baltica SH1, CAD74167.1) and ApPel1 ( Aspergillus parasiticus , KJK63907.1). The sequence alignment was performed by Vector-NTI. The three conserved residues coordinated with Ca 2+ are indicated by black dot. And the potential catalytic residues are marked with red triangle. Background colors represent different similarity: blue (conservative), green (block of similar) and yellow (identical), respectively

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques: Sequencing, Plasmid Preparation, Blocking Assay

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: The homology model of ErPelPL1 ( A ) and the key residues for substrate binding ( B )

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques: Binding Assay

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: The SDS-PAGE analysis of purified ErPelPL1. Lane left: molecular weight marker (Thermo Scientific, USA); lane 1: purified ErPelPL1

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques: SDS Page, Purification, Molecular Weight, Marker

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: Biochemical characterization of ErPelPL1. A The optimal temperature of ErPelPL1. B The thermal stability of ErPelPL1. C The optimal pH of ErPelPL1. D The pH stability of ErPelPL1. E The optimal Ca 2+ concentration of ErPelPL1. F The effects of various metal ions and reagents on ErPelPL1. Each value represents the mean of three replicates ± standard deviation. The enzymatic activity without adding metal ions or reagents was designated as 100% served as the control

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques: Concentration Assay, Standard Deviation, Activity Assay, Control

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: TLC analysis of the ErPelPL1 hydrolyzed products for different times. Lanes 1–12, the samples taken by 5 min, 10 min, 15 min, 30 min, 1 h, 2 h, 4 h, 6 h, 12 h, 24 h, 48 h and 72 h. Lane M, the oligosaccharide standards of d -galacturonic acid sodium salt

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques:

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: The FPLC analysis of ErPelPL1 degrading products. The reaction times are: 5 min, 30 min, 1 h, 6 h, 12 h, 24 h, 48 h, respectively. The eluents were detected by measuring the absorbance at 235 nm. The elution volumes of the unsaturated monomer, dimer, trimer, tetramer, pentamer and hexamer are 16.25, 15.23, 14.38, 13.61, 13.01, and 12.89 mL

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques:

Journal: Bioresources and Bioprocessing

Article Title: Elucidating the degradation pattern of a new cold-tolerant pectate lyase used for efficient preparation of pectin oligosaccharides

doi: 10.1186/s40643-021-00475-2

Figure Lengend Snippet: ESI-MS analysis of the degradation products of ErPelPL1 towards polygalacturonic sodium. The mass-to-charge ratios ( m/z ) of oligosaccharide products were detected by using ESI-MS. ΔDP n ( n = 1–6) represents unsaturated oligosaccharides with DP of 1–6

Article Snippet: The recombinant ErPelPL1 was purified by high-affinity Ni-charged resin FF (Ni–NTA Sepharose) prepacked column (GeneScript, Nanjing, China) and analyzed by SDS-PAGE (Fig. ).

Techniques: