Whey valorization using transgalactosylation activity of immobilized β‐galactosidase

Simović, Milica; Milivojević, Ana; Ćorović, Marija; Banjanac, Katarina; Bezbradica, Dejan

doi:10.1111/ijfs.14222

Cited by 16 publications

(8 citation statements)

References 48 publications

(65 reference statements)

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“…β-Galactosidases from Aspergillus oryzae, Kluyveromyces lactis , and Bacillus circulans are commonly used for commercial GOS production from lactose (Fischer & Kleinschmidt, 2021 ; Zerva et al., 2021 ). While these enzymes have been researched for GOS production from sweet and acid whey (Bolognesi et al., 2021 ; Fischer & Kleinschmidt, 2015 ; Mano et al., 2019 ; Simović et al., 2019 ), recent research has begun characterizing similar enzymes from other organisms such as Thermothielavioides terrestris (Zerva et al., 2021 ), Cryptococcus laurentii (Fischer & Kleinschmidt, 2021 ), and Pantoea anthrophila (Yañez-Ñeco et al., 2021 ). These enzymes have desirable properties such as greater thermostability, or better salt tolerance and low pH optima, which are especially useful for valorizing acid whey.…”

Section: Carbohydrate-rich Food Wastesmentioning

confidence: 99%

Microbial valorization of underutilized and nonconventional waste streams

Lad

Coleman

Alper

2021

Journal of Industrial Microbiology and Biotechnology

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The growing burden of waste disposal coupled with natural resource scarcity has renewed interest in the remediation, valorization and/or repurposing of waste. Traditional approaches such as composting, anaerobic digestion, use in fertilizers or animal feed, or incineration for energy production extract very little value out of these waste streams. In contrast, waste valorization into fuels and other biochemicals via microbial fermentation is an area of growing interest. In this review, we discuss microbial valorization of nonconventional, aqueous waste streams such as food processing effluents, wastewater streams, and other industrial wastes. We categorize these waste streams as carbohydrate-rich food wastes, lipid-rich wastes, and other industrial wastes. Recent advances in microbial valorization of these nonconventional waste streams are highlighted, along with a discussion of the specific challenges and opportunities associated with impurities, nitrogen content, toxicity, and low productivity.

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Section: Carbohydrate-rich Food Wastesmentioning

confidence: 99%

Microbial valorization of underutilized and nonconventional waste streams

Lad

Coleman

Alper

2021

Journal of Industrial Microbiology and Biotechnology

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“…However, since lactose is difficult to digest, most of it is discarded, which in turn seriously pollutes the environment. Lactose is hydrolyzed by β-galactosidase, and when its hydrolysis rate reaches 80%, it can be consumed or used as feed, thereby avoiding wastage of resources [5,7,8]. In addition, for humans, β-galactosidase is an important glycoside hydrolase responsible for hydrolyzing dietary lactose to produce galactose Molecules 2022, 27, 4497 2 of 15 and glucose [4].…”

Section: Introductionmentioning

confidence: 99%

Cloning, Expression, Purification, and Characterization of β-Galactosidase from Bifidobacterium longum and Bifidobacterium pseudocatenulatum

Yang

Jiang

et al. 2022

Molecules

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Expression and purification of β-galactosidases derived from Bifidobacterium provide a new resource for efficient lactose hydrolysis and lactose intolerance alleviation. Here, we cloned and expressed two β-galactosidases derived from Bifidobacterium. The optimal pH for BLGLB1 was 5.5, and the optimal temperature was 45 °C, at which the enzyme activity of BLGLB1 was higher than that of commercial enzyme E (300 ± 3.6 U/mg) under its optimal conditions, reaching 2200 ± 15 U/mg. The optimal pH and temperature for BPGLB1 were 6.0 and 45 °C, respectively, and the enzyme activity (0.58 ± 0.03 U/mg) under optimum conditions was significantly lower than that of BLGLB1. The structures of the two β-galactosidase were similar, with all known key sites conserved. When o-nitrophenyl-β-D-galactoside (oNPG) was used as an enzyme reaction substrate, the maximum reaction velocity (Vmax) for BLGLB1 and BPGLB1 was 3700 ± 100 U/mg and 1.1 ± 0.1 U/mg, respectively. The kinetic constant (Km) of BLGLB1 and BPGLB1 was 1.9 ± 0.1 and 1.3 ± 0.3 mmol/L, respectively. The respective catalytic constant (kcat) of BLGLB1 and BPGLB1 was 1700 ± 40 s−1 and 0.5 ± 0.02 s−1, respectively; the respective kcat/Km value of BLGLB1 and BPGLB1 was 870 L/(mmol∙s) and 0.36 L/(mmol∙s), respectively. The Km, kcat and Vmax values of BLGLB1 were superior to those of earlier reported β-galactosidase derived from Bifidobacterium. Overall, BLGLB1 has potential application in the food industry.

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“…Despite these activating effects of cations even at low concentrations, lower yields of galactooligosaccharides with different compositions were obtained in dairy whey systems, compared to lactose buffer solutions [14]. Recently, whey has been used for the production of galactooligosaccharides in some research; however, no results concerning the role of cations were included [15,16].…”

Section: Introductionmentioning

confidence: 99%