Characterization of the starch surface binding site on Bacillus paralicheniformis α-amylase

Božić, Nataša; Rozeboom, H.J.; Lončar, Nikola; Slavić, Marinela Šokarda; Janssen, Dick B.; Vujčić, Zoran

doi:10.1016/j.ijbiomac.2020.10.025

Cited by 23 publications

(29 citation statements)

References 65 publications

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“…2B ). They provide a hydrophobic platform for the carbohydrates while their substitutions with alanine resulted in 5-fold lower raw starch catalytic efficiency with more than 5.5-fold lower affinity compared to the wild type ( Boi et al, 2020 ).…”

Section: Survey Methodologymentioning

confidence: 99%

“…As illustrated in Fig. 2A , Bli Amy possessed four metal ion ligands: two calcium ions (Ca 2+ ) and two sodium ions (Na + ) ( Boi et al, 2020 ). Two calcium ions (CaI-CaII) and a sodium ion (NaI) formed a metal triad which was in the interior of Domain B, while NaII resided between Domain A and Domain C.…”

Section: Survey Methodologymentioning

confidence: 99%

“…As aforementioned, α-amylases have been grouped into 4 distinct families encompassing GH 13, GH 14, GH 57 and GH 119 with GH 13 accommodating highest number of α-amylases. Therefore, this section will discuss only on the structural properties of microbial α-amylases which fall in GH13 in CaZy database based on a recently elucidated structure of B. paralicheniformis ATCC 9945a α-amylase (Bli Amy) (Božić et al, 2020).…”

Section: Structural Properties Of Microbial α-Amylasesmentioning

confidence: 99%

“…Full-size DOI: 10.7717/peerj.11315/fig- 2 2A. Unlike CBM located usually at separate domains which connected to the N-or Ctermini of the catalytic domain (Domain A) via a polypeptide linker, SBS was a non-catalytic site present mostly in the catalytic domain, which enhanced the starch-absorptivity level and subsequently increased the raw starch degradation rates (Baroroh et al, 2017;Božić et al, 2020). In Bli Amy, the SBS which binds maltotetraose has two key amino acids F257 and Y358 (Fig.…”

Section: Structural Properties Of Microbial α-Amylasesmentioning

confidence: 99%

“…Figure23D crystal structure of B. paralicheniformis α-amylase (Bli Amy; PDB ID: 6TP1) with maltotetraose at its substrate-binding site (SBS)(Božić et al, 2020). (A) Bli Amy has a three-domain fold structure which is composed of Domain A, Domain B and Domain C as depicted in light blue, violet and wheat colours, respectively.…”

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Native to designed: microbial α-amylases for industrial applications

Lim

Oslan

2021

PeerJ

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Background α-amylases catalyze the endo-hydrolysis of α-1,4-D-glycosidic bonds in starch into smaller moieties. While industrial processes are usually performed at harsh conditions, α-amylases from mainly the bacteria, fungi and yeasts are preferred for their stabilities (thermal, pH and oxidative) and specificities (substrate and product). Microbial α-amylases can be purified and characterized for industrial applications. While exploring novel enzymes with these properties in the nature is time-costly, the advancements in protein engineering techniques including rational design, directed evolution and others have privileged their modifications to exhibit industrially ideal traits. However, the commentary on the strategies and preferably mutated residues are lacking, hindering the design of new mutants especially for enhanced substrate specificity and oxidative stability. Thus, our review ensures wider accessibility of the previously reported experimental findings to facilitate the future engineering work. Survey methodology and objectives A traditional review approach was taken to focus on the engineering of microbial α-amylases to enhance industrially favoured characteristics. The action mechanisms of α- and β-amylases were compared to avoid any bias in the research background. This review aimed to discuss the advances in modifying microbial α-amylases via protein engineering to achieve longer half-life in high temperature, improved resistance (acidic, alkaline and oxidative) and enhanced specificities (substrate and product). Captivating results were discussed in depth, including the extended half-life at 100 °C, pH 3.5 and 10, 1.8 M hydrogen peroxide as well as enhanced substrate (65.3%) and product (42.4%) specificities. These shed light to the future microbial α-amylase engineering in achieving paramount biochemical traits ameliorations to apt in the industries. Conclusions Microbial α-amylases can be tailored for specific industrial applications through protein engineering (rational design and directed evolution). While the critical mutation points are dependent on respective enzymes, formation of disulfide bridge between cysteine residues after mutations is crucial for elevated thermostability. Amino acids conversion to basic residues was reported for enhanced acidic resistance while hydrophobic interaction resulted from mutated hydrophobic residues in carbohydrate-binding module or surface-binding sites is pivotal for improved substrate specificity. Substitution of oxidation-prone methionine residues with non-polar residues increases the enzyme oxidative stability. Hence, this review provides conceptual advances for the future microbial α-amylases designs to exhibit industrially significant characteristics. However, more attention is needed to enhance substrate specificity and oxidative stability since they are least reported.

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Section: Survey Methodologymentioning

confidence: 99%

Section: Survey Methodologymentioning

confidence: 99%

Section: Structural Properties Of Microbial α-Amylasesmentioning

confidence: 99%

Section: Structural Properties Of Microbial α-Amylasesmentioning

confidence: 99%

mentioning

confidence: 99%

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Native to designed: microbial α-amylases for industrial applications

Lim

Oslan

2021

PeerJ

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Chemical characterization and biological abilities of Anthocleista djalonensis collected from two locations of Ivory Coast

Sinan

Zengin

Uba³

et al. 2023

eFood

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In this study, the total phenolic and flavonoid contents, HPLC‐DAD detected phytochemicals, antioxidant and enzyme inhibitory potential of methanolic and aqueous (as infusion) extracts of the medicinal plant, Anthocleista djalonensis (leaf and stem bark) collected from two locations, Mafiblé and Prikro, in Ivory Coast, were investigated. The ranges of total phenolic and flavonoid contents obtained were 14.17–46.95 mg gallic acid equivalent (GAE)/g and 2.96–34.76 mg rutin equivalent (RE)/g, respectively. Antioxidant abilities in terms of radical scavenging, reducing and metal chelating activity of the extracts in different assays were as follows: DPPH (4.90–48.82 mg trolox equivalent [TE]/g), ABTS (21.05–81.89 mg TE/g), CUPRAC (29.54–122.33 mg TE/g), FRAP (17.53–94.06 mg TE/g) and metal chelating (10.09–28.49 mg EDTAE/g. The extracts of A. djalonensis collected from Mafiblé, especially those of stem bark, contained higher level of total bioactive contents compared to Prikro extracts, detected by high‐performance liquid chromatography with photodiode‐array detection (HPLC‐DAD). Only the methanolic extracts irrespective of plant parts/location, showed inhibition against acetylcholinesterase (1.42–2.12 mg galantamine equivalent (GALAE)/g), while only the stem bark methanolic extract of A. djalonensis from Mafiblé was found to inhibit butyrylcholinesterase (0.65 mg GALAE/g). Thus, findings from this study could be useful for better application of the medicinal benefits from this plant.

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