β-galactosidase stability at high substrate concentrations

Warmerdam, Anja; Boom, R.M.; Janssen, A.E.M.

doi:10.1186/2193-1801-2-402

Cited by 28 publications

(27 citation statements)

References 21 publications

(32 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Palai et al () observed an increase in the formation of total GOS (i.e., the sum of DP3–5 fractions) from 22 to 39% as the initial lactose concentration increased from 55 to 525 g L −1 . Also, results of Warmerdam, Boom, et al () determined at 5 w/w% and 30 w/w% lactose concentration agree well with our observations under similar conditions but using different source of substrate. However, our results lay clearly below the high yields reported by Sen et al () for Biolacta FN5 using UF whey permeates in STR.…”

Section: Resultssupporting

confidence: 92%

“…Our results on GOS yields compare well with the yields reported for STR using buffered solutions of (pure) lactose (Palai et al, ; Warmerdam, Boom, & Janssen, ). Palai et al () observed an increase in the formation of total GOS (i.e., the sum of DP3–5 fractions) from 22 to 39% as the initial lactose concentration increased from 55 to 525 g L −1 .…”

Section: Resultssupporting

confidence: 90%

See 1 more Smart Citation

The impact of membrane pretreatment on the enzymatic production of whey‐derived galacto‐oligosaccharides

Pázmándi

Maráz

Ladányi

et al. 2017

J Food Process Engineering

View full text Add to dashboard Cite

This study presents a multistep process for the valorization of whey that involves membrane filtration techniques to fractionate whey compounds and the subsequent enzymatic conversion of lactose into galacto‐oligosaccharides with a degree of polymerization (DP) of 3–5. Partially demineralized whey was first concentrated and diafiltered by ultrafiltration (UF) to obtain whey protein isolates. Over 97% of the initial amount of lactose was recovered into the permeate which was then concentrated by nanofiltration (NF) up to 330 g L−1. Finally, a systematic study was performed to investigate the hydrolytic and transgalactosylation activity of Biolacta N5, a Bacillus circulans‐derived β‐galactosidase, on whey‐derived substrates consisting of lactose in various concentrations. Hydrolysis was especially pronounced for UF permeates with low lactose concentrations (< 50 g L−1), whereas transgalactosylation was dominant for streams concentrated by NF, obtaining comparable yields of the DP3‐5 fractions (∼ 35%) for moderate and high NF concentration factors. Practical applications The market for functional foods and dairy‐based functional beverages represents a growing segment of the global food industry. This article describes a technique for the valorization of whey that is based on the fractionation of whey constituents and the subsequent bioconversion of lactose into GOS. GOS are prebiotic substances with favorable technological properties such as low viscosity and good pH and temperature stability. These low‐calorie sweeteners can be added to a wide range of foods to increase product functionality. The here proposed multiproduct process has potential applications in whey management practice. The reported experimental data on the performance of the processing steps and the proposed approaches to the synchronization of the individual operations is useful for the design of whey valorization processes with reduced waste and energy consumption.

show abstract

Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 90%

The impact of membrane pretreatment on the enzymatic production of whey‐derived galacto‐oligosaccharides

Pázmándi

Maráz

Ladányi

et al. 2017

J Food Process Engineering

View full text Add to dashboard Cite

show abstract

“…Continuing fermentation, the glucose concentration decreased due to the formation of novel oligosaccharides (Cezar et al, 2018). As shown by several researchers (Bojan et al, 2011;Goderska et al, 2008;Warmerdam et al, 2013), lactose hydrolysis with Bifidobacterium bifidum β-galactosidase showed high activity significantly reducing initial lactose amount in substrates. It influences the final monosaccharides concentration, especially higher glucose yield.…”

Section: Figure 1 the Effect Of Fermentation Process On The Monosaccmentioning

confidence: 78%

The optimization of acid whey permeate hydrolysis for glucose-galactose syrup production

Samadov¹,

Ciproviča²,

Zolnere³

et al. 2019

Foodbalt

View full text Add to dashboard Cite

Whey contains a lot of lactose, which can be easily hydrolysed by commercial enzymes. The aim of the present study was to identify the optimal parameters for the enzymatic hydrolysis of acid whey permeate and glucose-galactose syrup production. Acid whey permeate was hydrolysed using β-galactosidase preparate (NOLA TM Fit 5500, Chr. Hansen, Denmark) with activity 7200 BLU L -1 . As the enzyme is strongly inhibited at pH below 4.5, sodium bicarbonate was added to neutralize substrate pH till 6.0-6.3. The hydrolysis was carried out at 40 °C 6 hours. pH and monosaccharides concentration were monitored during the process of hydrolysis. The fermented substrate was concentrated in a vacuum evaporator at 40-60 °C, 4-8 kPa. Glucose-galactose syrup was obtained with 65 and 70% of total solids. Lactose and monosaccharides were determined by HPLC. Fermentation time influenced monosaccharides composition and concentration. After 2 hours of fermentation lactose was completely hydrolysed. Continuing fermentation, the amount of glucose was decreased due to formation of novel oligosaccharides. The study results revealed that the optimal time for acid whey permeate hydrolysis was 2 hours. It should be noted that during the process of hydrolysis the pH of the product increased till 6.5 and such changes are related to cellulase and glucoamylase activity incorporated in the enzyme preparate as well as permeate protein residues hydrolysis. With the increase of syrup total solids, galactose concentration was changed due to galacto-oligosaccharides formation. The degree of sweetness is key factor for the durability of lactose hydrolysis and final syrup concentration.

show abstract

“…The enzyme showed increased stability in the presence of its substrate. Significant stability of inulinase for hydrolyzing inulin up to ten cycles at 60°C may be attributed to the conformational change or conformational tightening of enzyme in the presence of its substrate [13,26,28]. Decrease in the sugar yield after the first cycle could be due to the loss of loosely bound enzyme from its support material.…”

Section: Reusability Of Immobilized Biocatalyst For Inulin Hydrolysismentioning

confidence: 99%

Rapid and efficient bioconversion of chicory inulin to fructose by immobilized thermostable inulinase from Aspergillus tubingensis CR16

Trivedi

Divecha

Shah³

et al. 2015

Bioresour. Bioprocess.

View full text Add to dashboard Cite

Background: Fructose, a monosaccharide, has gained wide applications in food, pharmaceutical and medical industries because of its favourable properties and health benefits. Biocatalytic production of fructose from inulin employing inulinase is the most promising alternative for fructose production. For commercial production, use of immobilized inulinase is advantageous as it offers reutilization of enzyme and increase in stability. In order to meet the demand of concentrated fructose syrup, inulin hydrolysis at high substrate loading is essential. Results: Inulinase was immobilized on chitosan particles and employed for fructose production by inulin hydrolysis. Fourier transform infrared spectroscopy (FTIR) analysis confirmed linkage of inulinase with chitosan particles. Immobilized biocatalyst displayed significant increase in thermostability at 60 and 65°C. Statistical model was proposed with an objective of optimizing enzymatic inulin hydrolytic process. At high substrate loading (17.5 % inulin), using 9.9 U/g immobilized inulinase at 60°C in 12 h, maximum sugar yield was 171.1 ± 0.3 mg/ml and productivity was 14.25 g/l/h. Immobilized enzyme was reused for ten cycles. Raw inulin from chicory and asparagus was extracted and supplied in 17.5 % for enzymatic hydrolysis as a replacement of pure inulin. More than 70 % chicory inulin and 85 % asparagus inulin were hydrolyzed under optimized parameters at 60°C. Results of high performance liquid chromatography confirmed the release of fructose after inulin hydrolysis. Conclusions: The present findings prove potentiality of immobilized thermostable inulinase from Aspergillus tubingensis CR16 for efficient production of fructose syrup. Successful immobilization of inulinase on chitosan increased its stability and provided the benefit of enzyme reutilization. Box-Behnken design gave a significant model for inulin hydrolysis. Extraction of raw inulin from chicory and asparagus and their enzymatic hydrolysis using immobilized inulinase suggested that it can be a remarkable cost-effective process for large-scale fructose production.

show abstract

β-galactosidase stability at high substrate concentrations

Cited by 28 publications

References 21 publications

The impact of membrane pretreatment on the enzymatic production of whey‐derived galacto‐oligosaccharides

The impact of membrane pretreatment on the enzymatic production of whey‐derived galacto‐oligosaccharides

The optimization of acid whey permeate hydrolysis for glucose-galactose syrup production

Rapid and efficient bioconversion of chicory inulin to fructose by immobilized thermostable inulinase from Aspergillus tubingensis CR16

Contact Info

Product

Resources

About