A new bioprocess for the production of prebiotic lactosucrose by an immobilized β-galactosidase

Duarte, Lovaine Silva; Schöffer, Jéssie da Natividade; Lorenzoni, André Soibelmann Glock; Rodrigues, Rafael C.; Rodrigues, Eliseu; Hertz, Plinho Francisco

doi:10.1016/j.procbio.2017.01.015

Cited by 58 publications

(20 citation statements)

References 37 publications

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“…We speculated that there may be product or glucose inhibition. Recently, enzyme immobilization [33] and glucose oxidase addition [34] have been used for the continuous lactosucrose production with higher productivity. These techniques may increase the industrialization feasibility of lactosucrose biosynthesis.…”

Section: Effect Of the Substrate Concentration And Enzyme Amount On Lmentioning

confidence: 99%

Biocatalytic synthesis of lactosucrose using a recombinant thermostable β-fructofuranosidase from Arthrobacter sp. 10138

Chen

Deng

et al. 2020

Bioengineered

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As a prebiotics, lactosucrose plays an important role in maintaining human gastrointestinal homeostasis. In this study, a thermostable enzyme from Arthrobacter sp. 10138 was screened from six βfructofuranosidase-producing strains for the lactosucrose production and the coding gene was heterologously expressed in Escherichia coli for efficient expression. Recombinant βfructofuranosidase was purified and biochemically characterized by MALDI-TOFMS spectrometry. The transfructosylation product by this recombinant enzyme was determined to be lactosucrose rather than other oligosaccharides or polysaccharides by HPLC and LC-MS. Efficient extracellular secretion of β-fructofuranosidase was achieved by the optimization of signal peptide and induction conditions. It was found that with the signal peptide torT, the highest extracellular activity reached 111.01 U/mL, which was 38.4-fold higher than that with the OmpA signal peptide. Under the optimal conditions (pH 6.0, temperature 50°C, enzyme amount 40 μg/ml, sucrose 150 g/L and lactose 150 g/L), 109 g/L lactosucrose was produced with a molar conversion ratio of 49.3%. Here the thermostable βfructofuranosidase from Arthrobacter sp. 10138 can be used for efficient synthesis of lactosucrose, and this provides a good startpoint for the industrial production of lactosucrose in the future.

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Section: Effect Of the Substrate Concentration And Enzyme Amount On Lmentioning

confidence: 99%

Biocatalytic synthesis of lactosucrose using a recombinant thermostable β-fructofuranosidase from Arthrobacter sp. 10138

Chen

Deng

et al. 2020

Bioengineered

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“…The transfructosylation activity may allow the synthesis of additional FOS compounds, such as lactosucrose (4 G -β-D-galactosylsucrose, [ 62 ]) depending on the initial sugars. Moreover, certain β-galactosidases can also synthesize the lactosucrose [ 63 , 64 , 65 ]. In our study, analytical assays showed a trisaccharide compound with the same retention time and mass-to-charge ratio ( m/z 503.3) of the raffinose in the o NPG–sucrose containing reaction.…”

Section: Discussionmentioning

confidence: 99%

β-Galactosidase-Producing Isolates in Mucoromycota: Screening, Enzyme Production, and Applications for Functional Oligosaccharide Synthesis

Volford

Varga

Szekeres

et al. 2021

JoF

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β-Galactosidases of Mucoromycota are rarely studied, although this group of filamentous fungi is an excellent source of many industrial enzymes. In this study, 99 isolates from the genera Lichtheimia, Mortierella, Mucor, Rhizomucor, Rhizopus and Umbelopsis, were screened for their β-galactosidase activity using a chromogenic agar approach. Ten isolates from the best producers were selected, and the activity was further investigated in submerged (SmF) and solid-state (SSF) fermentation systems containing lactose and/or wheat bran substrates as enzyme production inducers. Wheat bran proved to be efficient for the enzyme production under both SmF and SSF conditions, giving maximum specific activity yields from 32 to 12,064 U/mg protein and from 783 to 22,720 U/mg protein, respectively. Oligosaccharide synthesis tests revealed the suitability of crude β-galactosidases from Lichtheimia ramosa Szeged Microbiological Collection (SZMC) 11360 and Rhizomucor pusillus SZMC 11025 to catalyze transgalactosylation reactions. In addition, the crude enzyme extracts had transfructosylation activity, resulting in the formation of fructo-oligosaccharide molecules in a sucrose-containing environment. The maximal oligosaccharide concentration varied between 0.0158 and 2.236 g/L depending on the crude enzyme and the initial material. Some oligosaccharide-enriched mixtures supported the growth of probiotics, indicating the potential of the studied enzyme extracts in future prebiotic synthesis processes.

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“…Protein immobilization has been used in solid subsidies as a biotechnological application technology for enzymes, which has various benefits over the usage of free types, such as facilitating isolation from the reaction medium and reuse (Duarte et al, 2017;Mateo et al, 2007). Generally, proteins linked to functional support groups are highly stable when protein degradation is limited to the medium.…”

Section: Enzymes Immobilization Mediated By Mtgase-catalyzed Bioconjugationmentioning

confidence: 99%

Current industrial applications of microbial transglutaminase: A review

Muhammad¹,

Al‐Adeeb²,

Al‐Ansi³

et al. 2021

IJAEMS

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Transglutaminases are commonly used in a number of manufacturing operations, including the food and pharmaceutical industry, owing to their protein cross-linking properties. Transglutaminases derived from animal tissues and lungs, which were the first origins of this enzyme, are being substituted out in preference of microbial sources, which are less expensive and simpler to generate and purify. Following the identification of microbial transglutaminase (MTGase), the enzyme was formulated for industrial purposes using a conventional fermentation process based on the bacterium S. mobaraensis. Many trials have been conducted in this area in order to improve enzyme efficiency for commercial purposes. Several hosts microorganisms such as E. coli, Y. lipolytica, S. lividans, P. pastoris and C. glutamicum gene expression studies were conducted for transglutaminase production. This study reflects on the MTGase application in two broad industries: food and biotechnology. The usage of mTGase is presented for many food classes, highlighting implementation possibilities and obstacles to further enhance end-product efficiency. Few applications in the textile and leather industry, as well as applications in the PEGylation reaction, the development of antibody drug conjugates, and regenerative medicine, are also addressed.

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A new bioprocess for the production of prebiotic lactosucrose by an immobilized β-galactosidase

Cited by 58 publications

References 37 publications

Biocatalytic synthesis of lactosucrose using a recombinant thermostable β-fructofuranosidase from Arthrobacter sp. 10138

Biocatalytic synthesis of lactosucrose using a recombinant thermostable β-fructofuranosidase from Arthrobacter sp. 10138

β-Galactosidase-Producing Isolates in Mucoromycota: Screening, Enzyme Production, and Applications for Functional Oligosaccharide Synthesis

Current industrial applications of microbial transglutaminase: A review

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