Lactase Production from Lactobacillus acidophilus

Akolkar, Sameer K.; Sajgure, A.; Lele, S. S.

doi:10.1007/s11274-005-0079-9

Cited by 27 publications

(10 citation statements)

References 8 publications

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“…Indigenous L. acidophilus isolated from fermented ragi was used in the present study (Akolkar et al 2005). This isolate was grown in 50 mL MRS broth in 250-mL Erlenmeyer flask and incubated at 37°C under stationary conditions.…”

Section: Microorganisms and Its Maintenancementioning

confidence: 99%

“…In our previous study, we have isolated a Lactobacillus acidophilus strain from fermented ragi (Eleusine coracana), found to be a potential β-galactosidase producer (Akolkar et al 2005(Akolkar et al , 2006. Since the strain was isolated from ragi, one would expect the microbial isolate to possess specific enzymatic characteristics in the carbohydrate metabolism.…”

Section: Introductionmentioning

confidence: 99%

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Production of Cell Membrane-Bound α- and β-Glucosidase by Lactobacillus acidophilus

Mahajan

Desai

Lele

2010

Food Bioprocess Technol

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Hydrolytic enzymes, viz. α-and β-glucosidase, were produced from indigenous isolate, Lactobacillus acidophilus, isolated from fermented Eleusine coracana. Production of these enzymes was enhanced by optimizing media using one factor at a time followed by response surface methodology. The optimized media resulted in a 2.5-and 2.1-fold increase in α-and β-glucosidase production compared with their production in basal MRS medium. Localization studies indicated 80% of the total activity to be present in the cell membrane-bound fraction. Lack of sufficient release of these enzymes using various physical, chemical, and enzymatic methods confirmed their unique characteristic of being tightly cell membrane bound. Enzyme characterization revealed that both α-and β-glucosidase exhibited optimum catalytic activity at 50°C and pH 6.0 and 5.0, respectively. K m and V max of α-glucosidase were 4.31 mM and 149 μmolmin −1 mL −1 for pnitrophenyl-α-D-glucopyranoside as substrate and 3.8 mM and 120 μmolmin −1 mL −1 for β-glucosidase using p-nitrophenyl-β-D-glucopyranoside as the substrate.

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Section: Microorganisms and Its Maintenancementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Production of Cell Membrane-Bound α- and β-Glucosidase by Lactobacillus acidophilus

Mahajan

Desai

Lele

2010

Food Bioprocess Technol

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“…Because we thought that the enzyme from Rahnella aquatilis 14-1 may be a novel type of β-galactosidase, we attempted to purify this respective enzyme the purification of the enzyme was conveniently done by chromatography, using Sephadex G-25 and DEAE-cellulose columns, which is often used for the purification of β-galactosidase (Hoyoux et al 2001;Fernandes et al 2002;Turkiewicz et al 2003;Akolkar et al 2005). The enzyme was purified until a single band had been obtained in 10% SDS-PAGE, which corresponded to a molecular mass of cca 60 kDa.…”

Section: Discussionmentioning

confidence: 99%

Isolation and identification of a strain producing cold-adapted β galactosidase, and purification and characterisation of the enzyme

Liu¹,

Shi²,

Wang³

et al. 2008

Czech J. Food Sci.

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Liu W.Y., Shi Y.W., Wang X.q., Lou K. (2008): Isolation and identification of a strain producing coldadapted β-galactosidase, and purification and characterisation of the enzyme. Czech J. Food Sci., 26: 284-290.Enzymes with high specific activities at low temperatures have potential uses in the food industry. Cold-adapted microorganisms are potentially useful sources of cold-active enzyme. To find cold-adapted β-galactosidase, we isolated several cold-adapted microorganisms from glacier zone soil. One cold-adapted β-galactosidase producing strain was obtained. The biochemical characteristics and the results of 16S rDNA sequencing identified the strain as Rahnella aquatilis. The enzyme was purified by column chromatography after which a single protein band migrating near 60 kDa was observed by means of SDS-PAGE. The β-galactosidase was optimally active at 35°C and at pH 6.5 when assayed with o-nitrophenyl-β-d-galactopyrano-side as substrate. The enzyme activity was sensitive to temperatures above 40°C and was undetectable at 45°C. Metal ions Mn 2+ and K + activated the enzyme while Cu 2+ , Zn 2+ , Fe 3 + , and Al 3+ inhibited the activity. The enzyme was also assayed for lactose hydrolysis. When milk is treated with the enzyme at 30°C for 2 h, the degree of lactose hydrolysis can reach 80%. It has, thus, potential applications in the food industry.

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“…Our results were consistent with previous studies in which the presence of lactose in media enhanced β-gal activity when compared to the presence of glucose. We found that the presence of lactose in the growth medium led to β-gal activity enhancement for bifidobacteria and L. acidophilus specifically, [11,12]. We also examined the effect of bile on β-gal activity and found an increase in enzyme activity when bile was included in the medium (Table 2).…”

Section: β-Gal Of Probiotic Supplements After Exposure To 3% Bile (W/v)mentioning

confidence: 93%

Determining ?-Galactosidase Activity of Commercially Available Probiotic Supplements

Johnson¹

2015

J Nutr Food Sci

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Consumer interest in probiotics has dramatically increased in recent years due to improved knowledge of the significant benefits imparted on human health. A specific health issue in which probiotics have been found advantageous is lactose intolerance. Probiotics have demonstrated the ability to act on ingested lactose due to the presence of lactase. The objective of this study was to assess the β-galactosidase (β -gal) activity of commercially available probiotics supplements in the market. Ten supplements were used in this study. Two capsules of each supplement were allowed to activate in MRS broth for 10-12 h. Cultures were then inoculated into TPY broth with lactose (induced) or glucose (uninduced) then incubated at 37°C. After bacterial growth reached the mid log phase (optical density 0.7-0.9; 610 nm), the procedures as outlined by Miller were followed. Activity of β-gal was quantified using the o-nitrophenyl-β-D-galactoside (ONPG) assay. The activity of β-gal in the uninduced group ranged between 0 and 800 Miller unit, whereas there as the induced group ranged from 1 to 1,120 Miller units. When induced, supplement #5 exhibited the strongest enzyme activity at 1,120 Miller units and supplement #10 exhibited the lowest activity. Similarly, supplement #3 exhibited the highest (800 Miller unit) and supplements #1, #2 and #10 did not show any β-gal activity with glucose. These findings indicate that β-gal activity in the ten tested supplements varies. Our results suggest that not all of the commercially available probiotic supplements have the same health benefits.

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Lactase Production from Lactobacillus acidophilus

Cited by 27 publications

References 8 publications

Production of Cell Membrane-Bound α- and β-Glucosidase by Lactobacillus acidophilus

Production of Cell Membrane-Bound α- and β-Glucosidase by Lactobacillus acidophilus

Isolation and identification of a strain producing cold-adapted β galactosidase, and purification and characterisation of the enzyme

Determining ?-Galactosidase Activity of Commercially Available Probiotic Supplements

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