Production of Food Grade β-Galactosidase from Artisanal Yogurt Strains

Tarı, Canan; Üstok, Fatma Işık; Harsa, Şebnem

doi:10.1080/08905430903562807

Cited by 7 publications

(2 citation statements)

References 26 publications

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“…The efficiency of different cell disruption methods on the extraction of intracellular β -galactosidase enzyme from Streptococcus thermophilus and Lactobacillus delbrueckii subsp . thermophilus has been tested [ 33 ]. Lysozyme enzyme treatment was determined as the most effective method, which resulted in approximately 1.5 and 10 times higher enzyme activity than glass bead and homogenization treatment, respectively.…”

Section: Microbial Sources Of Enzymementioning

confidence: 99%

Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

2010

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The enzyme β-galactosidase can be obtained from a wide variety of sources such as microorganisms, plants, and animals. The use of β-galactosidase for the hydrolysis of lactose in milk and whey is one of the promising enzymatic applications in food and dairy processing industries. The enzyme can be used in either soluble or immobilized forms but the soluble enzyme can be used only for batch processes and the immobilized form has the advantage of being used in batch wise as well as in continuous operation. Immobilization has been found to be convenient method to make enzyme thermostable and to prevent the loss of enzyme activity. This review has been focused on the different types of techniques used for the immobilization of β-galactosidase and its potential applications in food industry.

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Section: Microbial Sources Of Enzymementioning

confidence: 99%

Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

2010

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“…galactosidases with acidic pH optimums prevail in whey hydrolysis [1,2]. On the other hand, although numerous bacteria synthesize this enzyme, the industrial usage of bacterial β-galactosidases is scarce due to the fact that a few bacteria are regarded as a safe source [18][19][20]. Therefore, in recent years, lactic acid bacteria (LAB) have attracted great interest mostly because of their GRAS (generally recognized as safe) status, which allows the use of crude enzyme extracts, without the necessity of performing tedious purification protocols [21].…”

Section: Introductionmentioning

confidence: 99%

Characterization of β-galactosidase from Lactobacillus acidophilus: Stability and kinetic study

Carevic¹,

Vukasinovic-Sekulic²,

Banjanac³

et al. 2017

Adv techn

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β-Galactosidase is the industrially important enzyme that catalyzes both, lactose hydrolysis and synthesis of different bioactive galactosides. In this study, optimal conditions (fermentation temperature, inoculum concentration and lactose concentration) for accomplishing high yields of β-galactosidase activity from Lactobacillus acidophilus ATCC 4356, bacteria regarded as safe for human consumption, were investigated. Using the response surface methodology (RSM), it was concluded that the highest activity and specific activity were obtained by 2-day shake-flask culture fermentation at 28 °C, provided that the lactose content in the fermentation medium was 1.48%, and the inoculum concentration was 2.8%. The optimum temperature and pH for the obtained enzyme were 45 °C and 6.5, respectively. More importantly, these conditions simultaneously ensure a high enzyme stability. The Km and Vmax values were 0.44 mM and 25.64 mM/h (for o-nitrophenyl-β-D-galactopyranoside), and 3.79 mM and 3.10 mM/h (for lactose), and the substrate excess inhibition was not observed. On the other hand, the enzyme was inactivated in the presence of Ca 2+ , Ba 2+ , and Cu 2+ .

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Production of β-galactosidase from streptococcus thermophilus for galactooligosaccharides synthesis

et al. 2014

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Efficiency of different methods for disruption of Streptococcus thermophilus cells, isolated from different dairy products, to release β-galactosidase and synthesis of GOS by extracted enzyme using whey supplemented with different concentrations of lactose as a substrate was studied. Unlike most other studies on GOS synthesis which used only one method of cell disruption and only few microbial strains, we compared five different cell disruption methods and used 30 strains of S. thermophilus in order to find out the most effective method and efficient strain for production of β-galactosidase. Appreciable amount of GOS (53.45 gL −1 ) was synthesized at a lactose concentration of 30 %, using enzyme (10 U mL −1 of reaction medium), extracted from S. thermophilus within a very short incubation time of 5 h at a temperature of 40°C and pH 6.8. S. thermophilus is heavily employed in the preparation of fermented dairy products but this study extends the use of this organism for the production of GOS, a potential prebiotic.

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Production of Food Grade β-Galactosidase from Artisanal Yogurt Strains

Cited by 7 publications

References 26 publications

Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

Potential Applications of Immobilizedβ-Galactosidase in Food Processing Industries

Characterization of β-galactosidase from Lactobacillus acidophilus: Stability and kinetic study

Production of β-galactosidase from streptococcus thermophilus for galactooligosaccharides synthesis

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