Effect of gene dosage and incubation temperature on production of β-mannanase by recombinant Pichia pastoris

Tang, Shizhe; Lin, Fu-lai; Zheng, Jia; Zhou, Hongbo

doi:10.1007/s11771-019-3992-z

Cited by 5 publications

(3 citation statements)

References 44 publications

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“…Different volumes of 0.2 mol/L Na 2 HPO 4 and 0.1 mol/L citric acid were dissolved to obtain different pH Na 2 HPO 4 -citric acid buffers. The β-mannanase developed by our research group was purchased from Hunan Lerkam Biology Co., Ltd. (Changsha, China) [ 13 , 14 ].…”

Section: Methodsmentioning

confidence: 99%

“…Some researchers have developed more efficient enzymes [ 11 , 12 ]. Our research group has also developed an efficient β-mannanase that demonstrates activity up to 50,000 U/mL and strong thermal and acid stability [ 13 , 14 ]. However, the conventional enzymatic hydrolysis method also has some disadvantages: the enzyme cannot be reused, and it is not easy to separate the enzyme from the product, causing an increase in costs [ 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

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Enhanced Enzymatic Performance of β-Mannanase Immobilized on Calcium Alginate Beads for the Generation of Mannan Oligosaccharides

Chen,

Tian,

Zhou

et al. 2023

Foods

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Mannan oligosaccharides (MOSs) are excellent prebiotics that are usually obtained via the enzymatic hydrolysis of mannan. In order to reduce the cost of preparing MOSs, immobilized enzymes that demonstrate good performance, require simple preparation, and are safe, inexpensive, and reusable must be developed urgently. In this study, β-mannanase was immobilized on calcium alginate (CaAlg). Under the optimal conditions of 320 U enzyme addition, 1.6% sodium alginate, 2% CaCl2, and 1 h of immobilization time, the immobilization yield reached 68.3%. The optimum temperature and pH for the immobilized β-mannanase (Man-CaAlg) were 75 °C and 6.0, respectively. The Man-CaAlg exhibited better thermal stability, a high degree of pH stability, and less substrate affinity than free β-mannanase. The Man-CaAlg could be reused eight times and retained 70.34% of its activity; additionally, the Man-CaAlg showed 58.17% activity after 30 days of storage. A total of 7.94 mg/mL of MOSs, with 4.94 mg/mL of mannobiose and 3.00 mg/mL of mannotriose, were generated in the oligosaccharide production assay. It is believed that this convenient and safe strategy has great potential in the important field of the use of immobilized β-mannanase for the production of mannan oligosaccharides.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enhanced Enzymatic Performance of β-Mannanase Immobilized on Calcium Alginate Beads for the Generation of Mannan Oligosaccharides

Chen,

Tian,

Zhou

et al. 2023

Foods

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show abstract

“…Besides medium, the optimization of cultivation temperature is also required. The temperatures between 20 and 30 °C were frequently employed for the GAP promoter-based systems, , three temperature conditions (20, 25, and 30 °C) were examined for the production of porcine MG. Among the three temperature conditions, 30 °C was found to be the best for porcine MG expression (Figure D).…”

Section: Resultsmentioning

confidence: 99%

Efficient Secretory Expression and Purification of Food-Grade Porcine Myoglobin in Komagataella phaffii

Zhang

Zhao

Wang

et al. 2021

J. Agric. Food Chem.

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Myoglobin (MG) is one of the eukaryotic heme-binding proteins that is closely associated with the real color and metallic taste of meat and can be used as a color additive in artificial meat alternatives. However, the traditional extraction methods are expensive and time-consuming and the heterologous biosynthesis of MG has never been reported. Herein, we achieved the secretory expression of porcine MG by engineered Komagataella phaffii using the suitable host (X33), signal peptide (α-factor signal peptide), and modified constitutive promoter (G1 promoter). In addition, the fermentation conditions for MG production were optimized at shaking-flask level (BMGY medium with 40 mg/L of hemin, 30 °C) and at fermenter level (30% DO, feeding 150 mg/L of hemin), resulting in the highest titer of 285.42 mg/L MG in fed-batch fermentations. Furthermore, a purification method for food-grade MG was developed, which can obtain 0.22 mol of heme/mol of MG with 88.0% purity and 66.1% recovery rate.

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Low specific growth rate and temperature in fed-batch cultures of a beta-propeller phytase producing Pichia pastoris strain under GAP promoter trigger increased KAR2 and PSA1-1 gene expression yielding enhanced extracellular productivity

Herrera-Estala

Fuentes-Garibay

Guerrero-Olazarán

et al. 2022

Journal of Biotechnology

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Effect of gene dosage and incubation temperature on production of β-mannanase by recombinant Pichia pastoris

Cited by 5 publications

References 44 publications

Enhanced Enzymatic Performance of β-Mannanase Immobilized on Calcium Alginate Beads for the Generation of Mannan Oligosaccharides

Enhanced Enzymatic Performance of β-Mannanase Immobilized on Calcium Alginate Beads for the Generation of Mannan Oligosaccharides

Efficient Secretory Expression and Purification of Food-Grade Porcine Myoglobin in Komagataella phaffii

Low specific growth rate and temperature in fed-batch cultures of a beta-propeller phytase producing Pichia pastoris strain under GAP promoter trigger increased KAR2 and PSA1-1 gene expression yielding enhanced extracellular productivity

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