Synthesis of alkylgalactosides using whole cells of Bacillus pseudofirmus species as catalysts

Das-Bradoo, Sapna; Svensson, Ingvar L; Santos, Jorge A.N.; Plieva, Fatima M.; Mattìasson, Bo; Hatti‐Kaul, Rajni

doi:10.1016/j.jbiotec.2004.03.004

Cited by 31 publications

(15 citation statements)

References 36 publications

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“…Stevenson reported the large-scale production of alkyl galactosides, which are prepared from naturally occurring renewable sources (sugars and fatty alcohols), and are easily biodegradable and more stable under alkaline conditions than the corresponding sugar fatty acid esters. They are a group of non-ionic surfactants with a variety of applications in food products, detergents and cleaning agents, personal health products, fine chemicals, and pharmaceuticals [7]. Christian reported galactosylation of antibiotics such as chloramphenicol, which is a phosphodiesterase inhibitor and is applicable against vaginal mycoses [8].…”

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confidence: 99%

Purification and Characterization of a Novel β-Galactosidase with Transglycosylation Activity from Bacillus megaterium 2-37-4-1

Wang

et al. 2008

Appl Biochem Biotechnol

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A novel beta-galactosidase of 120 kDa (BgaBM) from Bacillus megaterium 2-37-4-1 was purified, and its gene (bgaBM) was analyzed and expressed. It displayed wide acceptor specificity for transglycosylation with a series of acceptors, including pentose, hexose, hydroxyl, and alkyl alcohol using o-nitrophenyl-beta-D-galactoside (ONPG) as a donor. BgaBM preferentially hydrolyzed ONPG in all tested substrates and showed maximum activity at pH 7.5-8.0 and 55 degrees C. It was stable at pH 6.0-9.0 below 40 degrees C. The K(m) and V(max) values for ONPG and lactose were 9.5 mM, 16.6 mM/min and 12.6 mM, 54.4 mM/min, respectively. The nucleotide sequence of the bgaBM gene consists of an ORF of 3,105 bp corresponding to 118 kDa protein, which indicates that BgaBM is a modular enzyme in the glycosyl hydrolase family 2, including conserved sugar-binding domain, acid-base catalyst, and immunoglobulin-like beta-sandwich domain. The possible acid/base and nucleophile sites of BgaBM were estimated to be E481 and E547, respectively. Furthermore, expression of the bgaBM gene in Escherichia coli and purification of the recombinant enzyme were performed. The recombinant enzyme showed similar biochemical characteristics to natural enzyme.

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confidence: 99%

Purification and Characterization of a Novel β-Galactosidase with Transglycosylation Activity from Bacillus megaterium 2-37-4-1

Wang

et al. 2008

Appl Biochem Biotechnol

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“…The biomass containing the tannase enzyme was separated from the fermentation broth by centrifuging the suspension at 5,500 g for 15 Min, washing twice with citrate buffer (0.1 M) of pH 5.0, and stored at 5°C in the form of a pellet. A requisite amount of biomass was taken, and 1.5 mL of 0.1 M citrate buffer (pH 5.0) was added and frozen at –20°C and lyophilized at –40°C without adding any lyoprotectants . The lyophilized powder was used as a biocatalyst for esterification.…”

Section: Methodsmentioning

confidence: 99%

“…Cell‐associated tannase represents a unique naturally immobilized form of tannase, which avoids expensive and laborious operation of isolation, purification, and immobilization. In addition, natural immobilization has a higher recovery and yield when compared with chemical or physical immobilization and naturally immobilized enzymes invariably exhibit very high stability against solvent toxicity, adverse pH, and temperature compared to the free enzyme .…”

Section: Introductionmentioning

confidence: 99%

Production of propyl gallate in nonaqueous medium using cell‐associated tannase of Bacillus massiliensis: Effect of various parameters and statistical optimization

Aithal

Belur

2013

Biotech and App Biochem

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Enzymatic synthesis of propyl gallate in an organic solvent was studied using cell-associated tannase (E.C. 3.1.1.20) of Bacillus massiliensis. Lyophilized biomass showing tannase activity was used as a biocatalyst. The influence of buffer pH and strength, water activity, temperature, biocatalyst loading, gallic acid concentration, and 1-propanol concentration was studied by the one-factor-at-a-time method. Subsequently, response surface methodology was applied based on a central composite design to determine the effects of three independent variables (biocatalyst loading, gallic acid concentration, and 1-propanol concentration) and their mutual interactions. A total of 20 experiments were conducted, and a statistical model was developed, which predicted the maximum propyl gallate yield of 20.28 μg/mL in the reaction mixture comprising 40.4 mg biocatalyst, 0.4 mM gallic acid, and 6.52 % (v/v) 1-propanol in 9.5 mL benzene at 30°C. The subsequent verification experiments established the validity of the model. Under optimal conditions, 25% conversion of gallic acid to propyl gallate was achieved on a molar basis. The absence of the need for enzyme purification and subsequent immobilization steps and good conversion efficiency makes this enzyme system an interesting one. Reports on the applications of bacterial whole cell systems for synthetic reactions in organic solvents are scarce, and perhaps this is the first report on bacterial cell-associated tannase-mediated esterification in a nonaqueous medium.

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“…It can alleviate the problems associated with whey disposal, lactose crystallization in frozen concentrated deserts and milk consumption by lactose-intolerant individuals [4]. ␤-Galactosidase from Escherichia coli, Bacillus circulans, Kluyveromyces lactis, Aspergillus oryzae, or Aspergillus niger were shown to have transgalactosylation reaction; lactose serves as galactosyl donor and an acceptor to form di to higher galacto-oligosaccharides [5][6][7]. Galacto-oligosaccharides are added to nutritional foods such as infant formula and yogurt in order to promote the growth and the establishment of beneficial bacteria bifidobacteria in the intestine [8,9].…”

Section: Introductionmentioning

confidence: 99%

Applications of β-gal-III isozyme from Bacillus coagulans RCS3, in lactose hydrolysis

Singh

Joshi²,

Bhatia

2011

International Journal of Biological Macromolecules

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Synthesis of alkylgalactosides using whole cells of Bacillus pseudofirmus species as catalysts

Cited by 31 publications

References 36 publications

Purification and Characterization of a Novel β-Galactosidase with Transglycosylation Activity from Bacillus megaterium 2-37-4-1

Purification and Characterization of a Novel β-Galactosidase with Transglycosylation Activity from Bacillus megaterium 2-37-4-1

Production of propyl gallate in nonaqueous medium using cell‐associated tannase of Bacillus massiliensis: Effect of various parameters and statistical optimization

Applications of β-gal-III isozyme from Bacillus coagulans RCS3, in lactose hydrolysis

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