Production of manno-oligosaccharides from locust bean gum using immobilized Penicillium occitanis mannanase

Blibech, Monia; Châari, Fatma; Bhiri, Fatma; Dammak, Ilyes; Ghorbel, Raoudha; Châabouni, Semia Ellouz

doi:10.1016/j.molcatb.2011.08.007

Cited by 19 publications

(24 citation statements)

References 37 publications

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“…Furthermore, this type of enzyme also play an important role in the production of mannooligosaccharides. Previous studies have confirmed the enzymatic hydrolysis of different substrates by -mannanase to produce mannooligosaccharides (Blibech et al, 2011;Jian et al, 2013;Wang et al, 2013).…”

Section: Introductionmentioning

confidence: 80%

Cloning of Partial β-Mannanase Gene from Indonesia Marine Bacteria Bacillus Subtilis LBF-005

Yopi¹,

Rahmani²,

Amaniyah³

et al. 2017

Squalen Bull. Marine Fisheries Postharvest Biotech.

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The strain LBF-005 from marine bacteria have been already isolated and screened for mannanase degrading enzyme in submerged fermentation process. This strain was further identified by using 16S rRNA identification and showed that bacterium is belong to Bacillus subtilis that could produce mannanase with activity around 9.5 U/mL. The optimum pH and temperature for the activity of crude enzyme for mannanase were 6.0 and 50 o C, respectively. Cloning of mannanase gene from B. subtilis was conducted using six primer / set designed based on the homology analysis conserved region of several mannanases from bacteria (Bacillus sp.) glycosyl hydrolase (GH) family 26. Optimization of PCR conditions was performed by gradient PCR to obtain PCR product of -mannanase gene. The PCR product was obtained by the third primer combination and was estimated to be around 972-bp. Analysis of the nucleotide sequence indicated that the sequence has similarity with mananase gene from other Bacillus sp., such as the B. subtilis strain W LY-12, B. subtilis strain W L-8, B. subtilis strain CICC 10260, B.subtilis strain CD-25, B.subtilis strain G1, and Bacillus sp. SW U60 about 98%, 98%, 98%, 98%, 97% and 95%, respectively.

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Section: Introductionmentioning

confidence: 80%

Cloning of Partial β-Mannanase Gene from Indonesia Marine Bacteria Bacillus Subtilis LBF-005

Yopi¹,

Rahmani²,

Amaniyah³

et al. 2017

Squalen Bull. Marine Fisheries Postharvest Biotech.

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“…Purified enzymes are often non-reusable and suffer from the environment pressure in the industrial production and storage [18,[43][44][45]. In this study, the EnoM could drive the β-galactosidase on the surface of S. thermophilus cells in vitro, achieving the reutilization of this enzyme.…”

Section: Discussionmentioning

confidence: 97%

Identification and characterization of a moonlighting protein-enolase for surface display in Streptococcus thermophilus

Xin

Guo

et al. 2020

Microb Cell Fact

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Background: Streptococcus thermophilus is an important food starter and receiving more attention to serve as cell factories for production of high-valued metabolites. However, the low yields of intracellular or extracellular expression of biotechnological and biomedical proteins limit its practical applications. Results: Here, an enolase EnoM was identified from S. thermophilus CGMCC7.179 with about 94% identities to the surface-located enolases from other Streptococcus spp. strains. The EnoM was used as an anchor to achieve surface display in S. thermophilus using GFP as a reporter. After respectively mixing the GFP-EnoM fusion protein or GFP with S. thermophilus cells in vitro, the relative fluorescence units (RFU) of the S. thermophilus cells with GFP-EnoM was 80-folds higher than that with purified GFP. The sharp decrease in the RFU of sodium dodecyl sulfate (SDS) pretreated cells compared to those of non-pretreated cells demonstrated that the membrane proteins were the binding ligand of EnoM. Furthermore, an engineered β-galactosidase (β-Gal) was also successfully displayed on the cell surface of S. thermophilus CGMCC7.179 and the relative activity of the immobilized β-Gal remained up to 64% after reused 8 times. Finally, we also demonstrated that EnoM could be used as an anchor for surface display in L. casei, L. bulgaricus, L. lactis and Leuconostoc lactis. Conclusion: To our knowledge, EnoM from S. thermophilus was firstly identified as an anchor and successfully achieved surface display in LAB. The EnoM-based surface display system provided a novel strategy for the enzyme immobilization.

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“…Mannanase of Penicillium occitanis was reported to lose 50% of its activity after 4-hour incubation at 60 °C. The immobilized β-mannanase of Penicillium occitanis retained 40% of its activity after 30 min of incubation at 70 °C (Blibech et al, 2011).…”

Section: Mannanase Characterizationmentioning

confidence: 99%

“…The ability of β-mananase to degrade glucomannan backbone depends on several factors, including number and distribution of the substituents on the backbone and the ratio of glucose and mannose (Mc Cleary et al, 1986). Recent studies reported that mannanase from certain bacteria can hydrolyze mannan into certain oligosaccharides, such as mannooligosaccharide production from palm kernel by mannanase of Brevibacillus borstelensis (Utami et al, 2013), also from copra pulp by recombinant of A. niger (Cuong et al, 2013), and from locust bean gum by using immobilized Penicillium occitanis mannanase (Blibech et al, 2011). Hydrolysis of porang glucomannan by mannanase of S. violascens BF 3.10 in this study produced the same products compared to hydrolysis of konjac flour by endo-β-mannanase MAN5 (Zhang et al, 2009).…”

Section: Analyzing Mannooligosaccharides By Using Tlc and Hplcmentioning

confidence: 99%

Enzymatic Hydrolysis of Porang by Streptomyces violascens BF 3.10 Mannanase for the Production of Mannooligosaccharides

Safitri

Meryandini

Yopi

2014

Med Pet

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Porang (Amorphophallus muelleriBlumeo C dengan aktivitas enzim sebesar 16.38 U/mL dan stabil pada suhu 4 °C selama 48 jam. Selama 5 jam waktu hidrolisis, reaksi dengan konsentrasi substrat 0,25%, 0,5%, dan 1% glukomanan porang yang dilarutkan dalam 10 mL enzim menghasilkan manooligosakarida dengan derajat polimerisasi 2-3. Visualisasi produk hidrolisis mengggunakan metode thin layer chromatography (TLC) dan high performance liquid chromatography (HPLC) menunjukkan bahwa jenis manooligosakarida yang dihasilkan adalah glukosa, manobiosa, manotriosa, dan manotetrosa. Derajat polimerisasi dan gula-gula sederhana yang terbentuk menunjukkan bahwa mananase S. violascens bekerja secara aktif mengatalisis reaksi hidrolisis ikatan 1,4-β-D-manosida dari rantai utama β-1,4-mannan sehingga menghasilkan gula-gula sederhana manooligosakarida.

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Production of manno-oligosaccharides from locust bean gum using immobilized Penicillium occitanis mannanase

Cited by 19 publications

References 37 publications

Cloning of Partial β-Mannanase Gene from Indonesia Marine Bacteria Bacillus Subtilis LBF-005

Cloning of Partial β-Mannanase Gene from Indonesia Marine Bacteria Bacillus Subtilis LBF-005

Identification and characterization of a moonlighting protein-enolase for surface display in Streptococcus thermophilus

Enzymatic Hydrolysis of Porang by Streptomyces violascens BF 3.10 Mannanase for the Production of Mannooligosaccharides

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