Biochemical and thermal properties of β-galactosidase enzymes produced by artisanal yoghurt cultures

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

doi:10.1016/j.foodchem.2009.08.022

Cited by 58 publications

(38 citation statements)

References 25 publications

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“…However, our study was lower than the values reported by Fuquay et al (2011);Batista et al (2008); Tamime and Robinson (2007) who noticed that a greater consumption of lactose was metabolized up to ~20-30% by bacterial of yogurt culture through 2 h of incubation in fermented milk. In contrast, Ustok et al (2010); Kreft et al (2001) using L. delbrueckii ssp. bulgaricus ATCC 11842 and S. thermophilus95/2 pure strains, indicated up to 60% of lactose hydrolyzed at the Linko et al (1998) reported that only about 45-68% of the lactose in the medium was utilized by S. thermophilus11F under the experimental conditions used.…”

Section: Resultsmentioning

confidence: 95%

“…These observations agree with Wang et al (1996) who reported that the activity of β-galactosidase depends on pH; it decreases rapidly at lower pH values. Also, Gueimonde et al (2002);Carević et al (2015); Ustok et al (2010) demonstrated that Lactobacillus acidophilus, L. delbrueckii ssp. bulgaricus, and S. thermophilus displayed significantly higher levels (P< 0.05) of β-galactosidase activity at pH 6.3 (activity over 90% of maximum) with an optimum at pH 6.0 -7.0 and then lose in activity as the pH decreased.…”

Section: Resultsmentioning

confidence: 99%

“…The bacterial strain cells in fermented camel milk samples were disrupted, according to the method of Ustok et al (2010) by adding one milliliter of a 1:10 dilution (w/v) of fermented camel milk in 0.05 M (pH 7.0) sodium phosphate buffer to a tube containing 0.2 ml of egg white lysozyme (50 mg/ml buffer) (EC 3.2.1.17 ≥ 40000 U/mg protein, Sigma); mixed and held in an ice-water for 30 min to lysing bacterial cells by hydrolyzing the peptidoglycan present in the bacterial cell walls. Cell lysis suspensions were centrifuged at 6000 rpm for 10 min at 4±1ºC to remove debris and whole cells.…”

Section: Measuring β-Galactosidase Activity Preparation Of Fermented mentioning

confidence: 99%

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ENHANCEMENT OF Β-Galactosidase ACTIVITY OF LACTIC ACID BACTERIA IN FERMENTED CAMEL MILK

Ibrahim

2018

Emir J Food Agric

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It is known that, the main problem associated with the production of fermented camel milk is the lower growth rate of lactic acid bacteria which caused many quality problems in the final product. The aim of this research was to enhance of β-galactosidase enzymatic activity of Lactobacillus delbrueckii ssp. bulgaricus DSMZ 20081, Streptococcus thermophilus ATCC 19258 and Lactobacillus acidophilus DSMZ 20079 by cell-rupture method to release their intracellular β-galactosidase and used the ruptured cell cultures as the source of the β-galactosidase enzyme. The results show that the bacterial growth rate in fermented camel milk made by using mixed cells of L. delbrueckii ssp. bulgaricus, S. thermophilus and L. acidophilus was 2 h faster than whole cells of the same strains. Moreover, the significant (P<0.05) faster dropping in pH-value to about 4.6 was observed in fermented camel milk made by using mixed cells of S. thermophilus, L. acidophilus and L. delbrueckii ssp. bulgaricus it was 4.65±0.02, 4.64±0.01and 4.63±0.01 during 4 h of fermentation time, respectively. Furthermore, the highest significance (P<0.05) activity of β-galactosidase was obtained during 4 h of fermentation in all fermented camel milk made by using mixed cells of L. delbrueckii ssp. bulgaricus, L. acidophilus and S. thermophilus it was about 1.97±0.12, 1.77±0.06 and 1.70±0.01 IU/ml, respectively. On the other hand, more rapid and efficient utilization of lactose was observed in fermented camel milk made by using mixed cells of S. thermophilus, L. acidophilus and L. delbrueckii ssp. bulgaricus during the first 2 h of incubation time and the higher degree of lactose hydrolysis reached the maximum approximately 37.69, 38.39 and 40.56 % at the end of 10h of incubation time, respectively. The present results revealed that enhance of microbial growth rate in fermented camel milk can be simultaneously achieved by a suitable rupture-cell method.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Section: Measuring β-Galactosidase Activity Preparation Of Fermented mentioning

confidence: 99%

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ENHANCEMENT OF Β-Galactosidase ACTIVITY OF LACTIC ACID BACTERIA IN FERMENTED CAMEL MILK

Ibrahim

2018

Emir J Food Agric

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“…In case of lysozyme the concentration of lysozyme used for the cell disruption was standardized and use of 10 mg of lysozyme per ml of the cell suspension was found to be suitable for cell disruption. In some other studies, 22 mg of lysozyme per ml of the cell suspension was used for cell disruption Ustok et al 2010). In glass beads and sonication, the time required to disrupt the cells was standardized.…”

Section: Discussionmentioning

confidence: 99%

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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“…A partir da Tabela 1 podemos observar que com o aumento da temperatura ocorre um leve decréscimo nos valores de energia livre de Gibbs (∆G*). Todos os valores de ∆G* estão na ordem de magnitude esperada para desnaturação proteica 9 . Os valores ∆H* e ∆S* (Tabela 1) obtidos no presente estudo, também estão de acordo com o esperado para enzimas desnaturadas pelo calor.…”

Section: Bbr -Biochemistry and Biotechnology Reports -Issn 2316-5200 unclassified

Propriedades Termodinâmicas da Enzima Beta-Galactosidase Imobilizada em Eupergit® C

Braga¹,

Silveira²,

Kalil³

2013

BBR - Biochem. Biotechnol.

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INTRODUÇÃOA β-galactosidase é uma enzima hidrolítica com capacidade de transferase para grupos galactosil, atuando no resíduo terminal β-galactopiranosil da lactose para formar seus monossacarídeos glicose e galactose. É utilizada na indústria farmacêutica e alimentícia principalmente na elaboração de produtos destinados a pessoas com intolerância à lactose 1 . A lactose é um dissacarídeo que tem como características principais, baixa solubilidade em água e baixo poder adoçante. A cristalização deste açúcar em produtos lácteos, como leite condensado, e a restrição ao consumo de tais alimentos por pessoas intolerantes a este carboidrato, devido a baixos níveis de β-galactosidase intestinal, podem ser evitadas através do processo de hidrólise enzimático 1 . Dentre as fontes de β-galactosidase destacam-se aquelas obtidas por micro-organismos, principalmente a partir de leveduras do gênero Kluyveromyces, que são considerados seguros, podendo ser utilizados na área de alimentos 2,3 . A imobilização de β-galactosidase é uma ferramenta muito poderosa para melhorar quase todas as suas propriedades, incluindo estabilidade, atividade, seletividade, especificidade e redução de inibição 4 . Nesse contexto, o objetivo desse trabalho foi determinar algumas propriedades enzimáticas da enzima β-galactosidase parcialmente purificada e imobilizada, utilizando Eupergit ® C como suporte. MATERIAL E MÉTODOS Produção, Extração e Purificação da enzima β-galactosidase

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Biochemical and thermal properties of β-galactosidase enzymes produced by artisanal yoghurt cultures

Abstract: , respectively. Moreover, thermodynamic (DG, DS, DH) and kinetic constants (K m and V max ) were determined and effects of metal ions were investigated. As a result, these enzymes could be considered as potential candidates for lactose hydrolysis of milk and milk products.

Cited by 58 publications

References 25 publications

ENHANCEMENT OF Β-Galactosidase ACTIVITY OF LACTIC ACID BACTERIA IN FERMENTED CAMEL MILK

ENHANCEMENT OF Β-Galactosidase ACTIVITY OF LACTIC ACID BACTERIA IN FERMENTED CAMEL MILK

Production of β-galactosidase from streptococcus thermophilus for galactooligosaccharides synthesis

Propriedades Termodinâmicas da Enzima Beta-Galactosidase Imobilizada em Eupergit® C

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