Nowadays acrylamide is known not only as synthetic material used in industry, but also as carcinogenic, cyto- and genotoxic compound which forms during heat-induced process (due to Maillard reaction) mostly in foodstuff such as potato, bakery, plant derivatives products and coffee. The International Agency for Research on Cancer in 1994 declared acrylamide as a probable carcinogenic agent in humans. After metabolic process, acrylamide is distributed to all organs and tissues in human body. Acrylamide is classified as human neurotoxin, because this effect was observed in humans occupationally exposed to this compound. Acrylamide was found to cause apoptosis by mitochondrial dysfunction. Methods of acrylamide inactivation by microorganisms and bioactive diet compounds have also been reviewed. Moreover, there is still deficit of the European Union legal regulation concerning acrylamide mitigation strategies in food. Regulation 2017/2158 from 20 November 2017 is a step in the right direction when it comes to ensuring food safety and maximum levels of acrylamide in foodstuffs, however when exceeding those, it should result in elimination of such food from the market.

Acrylamide in human diet, its metabolism, toxicity, inactivation and the associated European Union legal regulations in food industry.

Marine microbial L-asparaginase: Biochemistry, molecular approaches and applications in tumor therapy and in food industry.

L-asparaginase (E.C.3.5.1.1) hydrolyzes L-asparagine to L-aspartic acid and ammonia, which has been widely applied in the pharmaceutical and food industries. Microbes have advantages for L-asparaginase production, and there are several commercially available forms of L-asparaginase, all of which are derived from microbes. Generally, L-asparaginase has an optimum pH range of 5.0–9.0 and an optimum temperature of between 30 and 60 °C. However, the optimum temperature of L-asparaginase from hyperthermophilic archaea is considerable higher (between 85 and 100 °C). The native properties of the enzymes can be enhanced by using immobilization techniques. The stability and recyclability of immobilized enzymes makes them more suitable for food applications. This current work describes the classification, catalytic mechanism, production, purification, and immobilization of microbial L-asparaginase, focusing on its application as an effective reducer of acrylamide in fried potato products, bakery products, and coffee. This highlights the prospects of cost-effective L-asparaginase, thermostable L-asparaginase, and immobilized L-asparaginase as good candidates for food application in the future.

Microbial L-asparaginase for Application in Acrylamide Mitigation from Food: Current Research Status and Future Perspectives.

l-asparaginase (ASNase, EC 3.5.1.1) is an aminohydrolase enzyme with important uses in the therapeutic/pharmaceutical and food industries. Its main applications are as an anticancer drug, mostly for acute lymphoblastic leukaemia (ALL) treatment, and in acrylamide reduction when starch-rich foods are cooked at temperatures above 100 °C. Its use as a biosensor for asparagine in both industries has also been reported. However, there are certain challenges associated with ASNase applications. Depending on the ASNase source, the major challenges of its pharmaceutical application are the hypersensitivity reactions that it causes in ALL patients and its short half-life and fast plasma clearance in the blood system by native proteases. In addition, ASNase is generally unstable and it is a thermolabile enzyme, which also hinders its application in the food sector. These drawbacks have been overcome by the ASNase confinement in different (nano)materials through distinct techniques, such as physical adsorption, covalent attachment and entrapment. Overall, this review describes the most recent strategies reported for ASNase confinement in numerous (nano)materials, highlighting its improved properties, especially specificity, half-life enhancement and thermal and operational stability improvement, allowing its reuse, increased proteolysis resistance and immunogenicity elimination. The most recent applications of confined ASNase in nanomaterials are reviewed for the first time, simultaneously providing prospects in the described fields of application.

https://www.mdpi.com/1420-3049/25/24/5827/pdf

Recent Strategies and Applications for l-Asparaginase Confinement

Characterization of a novel type I l-asparaginase from Acinetobacter soli and its ability to inhibit acrylamide formation in potato chips

Biochemical characterization of a novel L-asparaginase from Paenibacillus barengoltzii being suitable for acrylamide reduction in potato chips and mooncakes.

Fucosyllactoses have gained much attention owing to their multiple functions, including prebiotic, immune, gut, and cognition benefits. In this study, human milk oligosaccharide (HMO) 2′-fucosyllactose (α-L-Fuc-(1,2)-D-Galβ-1,4-Glu, 2′FL) and its isomer 3′-fucosyllactose (α-L-Fuc-(1,3)-D-Galβ-1,4-Glu, 3′FL) with potential prebiotic effect were synthesized efficiently by a novel recombinant α-L-fucosidase. An α-L-fucosidase gene (PbFuc) from Pedobacter sp. CAU209 was successfully cloned and expressed in Escherichia coli (E. coli). The deduced amino acid sequence shared the highest identity of 36.8% with the amino sequences of other reported α-L-fucosidases. The purified α-L-fucosidase (PbFuc) had a molecular mass of 50 kDa. The enzyme exhibited specific activity (26.3 U/mg) towards 4-nitrophenyl-α-L-fucopyranoside (pNP-FUC), 3′FL (8.9 U/mg), and 2′FL (3.4 U/mg). It showed the highest activity at pH 5.0 and 35 °C, respectively. PbFuc catalyzed the synthesis of 3′FL and 2′FL through a transglycosylation reaction using pNP-FUC as donor and lactose as acceptor, and total conversion ratio was up to 85% at the optimized reaction conditions. The synthesized mixture of 2′FL and 3′FL promoted the growth of Lactobacillus delbrueckii subsp. bulgaricus NRRL B-548, L. casei subsp. casei NRRL B-1922, L. casei subsp. casei AS 1.2435, and Bifidobacterium longum NRRL B-41409. However, the growths of E. coli ATCC 11775, S. enterica AS 1.1552, L. monocytogenes CICC 21635, and S. aureus AS 1.1861 were not stimulated by the mixture of 2′FL and 3′FL. Overall, our findings suggest that PbFuc possesses a great potential for the specific synthesis of fucosylated compounds.

Biochemical characterization of a novel α-L-fucosidase from Pedobacter sp. and its application in synthesis of 3'-fucosyllactose and 2'-fucosyllactose

Lactic acid bacteria (LAB) are important in food fermentation and may enhance overall host health. Previous studies to explore LAB metabolism mainly focused on the genera Lacticaseibacillus and Lactococcus. Pediococcus pentosaceus, historically recognized as an important food fermentation bacterial strain, can produce bacteriocins and occasionally demonstrated probiotic functionalities. This study thoroughly surveyed the growth kinetic of three P. pentosaceus isolates in various culture formulations, especially in fructooligosaccharide (FOS), xylooligosaccharide (XOS), or konjac mannooligosaccharide (KMOS) conditions. Results showed that P. pentosaceus effectively metabolized KMOS, the culture of which led to 23.6-fold population increase. However, FOS and XOS were less metabolized by P. pentosaceus. On functional oligosaccharide cultures, P. pentosaceus could result in higher population proliferation, more acidified fermentation environment, and higher glycoside hydrolysis activities in the culture. RNA-Seq analysis classified 1572 out of 1708 putative genes as mRNA-coding genes. The dataset also revealed that the three functional oligosaccharides led to extensive global functional gene regulations. Phosphate conservation and utilization efficiency enhancement may serve as a leading transcriptional regulation direction in functional oligosaccharide metabolisms. In summary, these discovered metabolic characteristics could be employed to support future studies. KEY POINTS: • Konjac mannooligosaccharides effectively promoted P. pentosaceus proliferation. • Functional genes were highly regulated in functional oligosaccharide utilization. • Phosphate conservation was an important transcriptional regulation direction.

Global transcriptomic analysis of functional oligosaccharide metabolism in Pediococcus pentosaceus

Biochemical characterization of a β-N-acetylhexosaminidase from Catenibacterium mitsuokai suitable for the synthesis of lacto-N-triose II

A xyloglucanase gene (RmXEG12B) was cloned from Rhizomucor miehei CAU432 and successfully expressed in Pichia pastoris. The highest xyloglucanase activity of 26,200 U/mL was achieved after 168 h high-cell-density fermentation. The optimal pH and temperature of RmXEG12B were 5.0 and 55°C, respectively. RmXEG12B showed good stability within pH of 3.0–10.0 and was stable up to 50°C. It exhibited the highest specific activity (5989.3 U/mg) towards tamarind xyloglucan. RmXEG12B hydrolyzed apple pomace xyloglucan to produce the partially hydrolyzed apple pomace xyloglucan, which demonstrated a weight average molecular weight of 1.6 × 104 Da and contained three major oligosaccharides with a degree of polymerization of 7–10. This is a strategy for the comprehensive utilization of apple pomace to produce the partially hydrolyzed apple pomace xyloglucan. 

High‐level expression of xyloglucanase B from
 Rhizomucor miehei
 and its application in the preparation of partially hydrolyzed apple pomace xyloglucan

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Biochemical characterization of a novel L-asparaginase from Paenibacillus barengoltzii being suitable for acrylamide reduction in potato chips and mooncakes.

Biochemical characterization of a novel α-L-fucosidase from Pedobacter sp. and its application in synthesis of 3'-fucosyllactose and 2'-fucosyllactose

Global transcriptomic analysis of functional oligosaccharide metabolism in Pediococcus pentosaceus

Biochemical characterization of a β-N-acetylhexosaminidase from Catenibacterium mitsuokai suitable for the synthesis of lacto-N-triose II

High‐level expression of xyloglucanase B from Rhizomucor miehei and its application in the preparation of partially hydrolyzed apple pomace xyloglucan