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Cosme, F.; Inês, A.; Vilela, A. Microbial and Commercial Enzymes in Beverage Production Process. Encyclopedia. Available online: https://encyclopedia.pub/entry/43764 (accessed on 10 August 2024).
Cosme F, Inês A, Vilela A. Microbial and Commercial Enzymes in Beverage Production Process. Encyclopedia. Available at: https://encyclopedia.pub/entry/43764. Accessed August 10, 2024.
Cosme, Fernanda, António Inês, Alice Vilela. "Microbial and Commercial Enzymes in Beverage Production Process" Encyclopedia, https://encyclopedia.pub/entry/43764 (accessed August 10, 2024).
Cosme, F., Inês, A., & Vilela, A. (2023, May 04). Microbial and Commercial Enzymes in Beverage Production Process. In Encyclopedia. https://encyclopedia.pub/entry/43764
Cosme, Fernanda, et al. "Microbial and Commercial Enzymes in Beverage Production Process." Encyclopedia. Web. 04 May, 2023.
Microbial and Commercial Enzymes in Beverage Production Process
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This entry is adapted from the peer-reviewed paper 10.3390/fermentation9040385

Enzymes are highly effective biocatalysts used in various industrial processes, playing a key role in winemaking and in other fermented beverages. Many of the enzymes used in fermentation processes have their origin in fruits, in the indigenous microbiota of the fruit, and in the microorganisms present during beverage processing. Besides naturally occurring enzymes, commercial preparations that usually blend different activities are used (glucosidases, glucanases, pectinases, and proteases, among others).

enzymes glucosidases glucanases pectinases grape-berry yeasts lactobacillus

1. Introduction

Enzymes are biocatalysts that accelerate biochemical reactions in living organisms. They can also be extracted from cells and used to catalyse several important industrial processes [1]. Enzymes were discovered in the second half of the nineteenth century, and in 1878, the German physiologist Wilhelm Kühne was the first scientist to use the word ‘enzyme’ when explaining the process of sugars fermentation by yeast. The word derives from the Greek words en (meaning ‘within’) and zume (meaning ‘yeast’) [1].
Enzymes are, normally, globular proteins and consist of long linear chains of amino acids that fold to produce a three-dimensional structure. Enzymes are extremely efficient and highly specific biocatalysts playing a pivotal role in the beverage production processes. For example, in wine production, many of the biotransformations occurred by employing the enzymes produced in the indigenous microflora on the grape and in the microorganisms present in the winemaking [2][3].
With the advance of biotechnology and the understanding of the function of enzymes, commercial enzyme preparations are nowadays used at different stages of the process in the beverage industry (alcoholic and non-alcoholic beverages) to obtain better quality products [3][4][5]. For example, they are used to accelerate solid settling and clarification and improve colour extraction, and they can also be used for achieving better extraction performances by increasing juice yield and increasing processing efficiency such as pressing [6]. Commercial enzyme preparations act like the natural enzymes from grapes and yeast, but with improved selectivity, activity, and stability under operational conditions [3]. In the beverage industry, the application of enzymes is a gainful option, which improves yields and, at the same time, reduces carbon footprint, energy consumption, and environmental pollution [7][8][9].
Enzymes can be used as food additives and/or processing aids. Most of them are used as processing aids, whereas others, such as lysozyme and invertase, are used as additives [10]. Among all groups of food and beverage enzymes, amylases, pectinases, and cellulases are extensively used in the beverage industry [8].

2. Enzymes Produced by Fungi (Moulds and Yeasts) in the Beverage Industry

According to Markets and Markets [11], the food enzymes market is forecasted to grow by $914.04 mn during 2022–2027, accelerating at a CAGR of 6.28% during the forecast period. The advancements in R&D, environmental concerns, and urbanisation, among others, led to the growth of this market. In addition, the progressions in technology (enzyme engineering, introduction of genetically engineered enzymes) have increased the growth of the food industry. Enzymes are used in various food applications, including baking, brewing, dairy, oil/fats, beverage, juice, and wine [12], and most of the commercial enzymes used in food and beverages are mass-produced using fungal hosts—both yeasts (unicellular) and filamentous fungi (multicellular), Table 1.
Table 1. List of approved enzyme activity for use as processing aids in food in Europe. For each product, the fungal or bacterial origin of the host organism is shown (colonies formed on Petri dishes in Potato-Dextrose Agar-PDA). Adapted from [13].

Enzyme Activity

Production

Microorganism

Host Organism

Morphology of Colonies

Aminopeptidase, Arabinofuranosidase, Catalase, Cellulase, Glucanase (endo-beta), Glucanase (exo-beta), Glucanase (beta), Glucoamylase, Glucose oxidase, Lactase or galactosidase (beta), Lysophospholipase, Pectinase, Xylanase

Aspergillus niger

Fermentation 09 00385 i001

Aminopeptidase (leucyl), Protease, Tannase

Aspergillus oryzae

Fermentation 09 00385 i002

AMP deaminase, Protease (exopeptidase)

Aspergillus melleus and Aspergillus usamii

Fermentation 09 00385 i003

Cellulase, Ribonuclease

Penicillium funiculosum

Fermentation 09 00385 i004

Cellulase, Glucanase (exo-beta), Xylanase

Trichoderma reesei

Fermentation 09 00385 i005

Dextranase

Chaetomium erraticum

Fermentation 09 00385 i006

Glucanase (beta)

Talaromyces emersonii

Not. available

Lipase triacylglycerol

Candida rugosa

Fermentation 09 00385 i007

Lipase triacylglycerol, Glucanase (endo-beta), Glucanase (exo-beta)

Rhizopus niveus

Fermentation 09 00385 i008

Lipase triacylglycerol

Rhizopus oryzae

Fermentation 09 00385 i009

Protease (mucorpepsin)

Rhizomucor miehei

Fermentation 09 00385 i010

Glucanase (beta), Xylanase

Humicola insolens

Not available
The yeast Saccharomyces cerevisiae has been widely used for food and alcoholic drinks due to its ability to ferment sugars into ethanol and carbon dioxide. Filamentous fungi or moulds have also been used for food and beverage production. As an example, miso is a traditional Japanese seasoning processed using Aspergillus oryzae and A. sake for the fermentation of soybean, barley, or rice. However, fungi can also be an important component of the final food product (Penicillium roqueforti strains used in blue cheese) [13]. In 1894, the manufacturing of an enzyme complex from A. oryzae was developed to produce different enzyme products in submerged fermentation [13]. However, the development of commercial sources of glucoamylase was the basis for the enzyme revolution in the starch industry [14].
From Table 1, some fungal enzymes can be exemplified, such as: (i) Glucoamylases (EC 3.2.1.3) that are exo-acting enzymes that catalyse the hydrolysis of polysaccharide starch from the non-reducing end, releasing β-glucose. These enzymes are produced by Aspergillus niger, A. awamori, and Rhizopus oryzae and are widely used for industrial applications [15]. They are found in a wide range of applications in the beverage industry, such as the production of sweet syrups (high-glucose and high-fructose), and play an important role in the production of sake, soya sauce, as well as light beer [16]. (ii) Acidic protease from Aspergillus usamii has been employed for the enhancement of functional properties of wheat gluten, allowing the release of peptides and amino acids for proper fermentation, not only for bread making but also for beer making, as they are efficient even at low pH by balancing the amino acid profile of beer [16][17]. (iii) Lipases, produced by A. niger or A. oryzae, are used in wine production to modify wine aroma [16]. (iv) Pectinolytic enzymes (polygalacturonase and pectase) are produced by Aspergillus spp. and are widely used for juice clarification, increasing juice yield prior to the grapes’ fermentation [18]. Invertase is produced from Saccharomyces spp. cells through the application of a proteolytic enzyme [18].

3. Enzymes Produced by Lactic Acid Bacteria in the Beverage Industry

Lactic acid bacteria (LAB) constitute one of the most important and relevant microbial groups in the food area due to their role in the production and quality of a diverse myriad of foods dispersed worldwide. This is the result of a complex metabolic activity. Thus, these bacteria are a huge source of enzymes, and their status as Generally Recognized as Safe (GRAS) microorganisms will help in this purpose. The only limitation that may compromise the industrial production of enzymes extracted from LAB is the slow growth of some strains, particularly ones isolated from wines—hence their direct use in wines to obtain the intended and desired biochemical transformations. Indeed, using whole cells, rather than purified enzymes, provides a series of advantages since whole cells are a natural environment for enzymes, preventing loss of activity in non-conventional media, and they can efficiently regenerate co-factors [19][20].
The main enzymes of wine LAB strains are the Malolactic enzymes, Glycosidases, Esterases, Lipases, Proteases, and Tannases.
Malolactic Enzyme-EC. 4.1.1.101– Malolactic Fermentation (MLF) is defined as the biotransformation of L-malic acid to L-lactic acid and carbon dioxide by the malolactic enzyme that exists in all LAB strains (formerly Lactobacillus, Pediococcus, Leuconostoc, and predominantly Oenococcus) isolated from grapes, must, and wine samples. This secondary fermentation, which usually occurs after alcoholic fermentation has been completed, is equally very important in red wines and specific wines and results in significant physicochemical and sensory modifications [21][22]. In addition to deacidification (the immediate effect of a decrease in acidity by the transformation of a dicarboxylic acid (L-malic acid), which is characterised by a harsh taste, into a monocarboxylic acid (L-lactic acid) with a milder taste) of the wine, with concomitant modification of its gustatory and olfactory perception, MLF contributes significantly to microbial stability (by the removal of L-malic acid, a potential carbon source for some spoilage microorganisms [23][24]) and often to the improvement of the sensory profile of wines. Modifications in wine aroma by LAB are due to L-lactic acid, less aggressive to the palate, but also due to a huge number of other compounds, such as diacetyl, acetoin, 2,3-butanediol, ethyl lactate, and diethyl succinate esters, and some higher alcohols and aromatic aglycones that become free by the action of LAB β-glucosidases [25][26][27][28].
Glycosidases-EC 3.2.1.21 β-D-Glucoside glucohydrolases; (Glycosidasic activity)—The varietal aroma of wines is given by volatile compounds that are mostly found in grapes in the form of non-volatile odourless molecules conjugated with monoglycosides (β-D-glucose) and diglycoside (β-D-glucose and a second sugar unit of α-L-arabinofuranose, α-L-rhamnopyranose, β-D-xylopyranose, or β-D-apiofuranose) [29]. Different classes of volatiles, including monoterpenes and C13-norisoprenoids, are the aglycon moiety that constitutes these glycoconjugate compounds. Although the acidic hydrolysis during wine ageing can transform them into free volatile aroma compounds, a slow process and faster enzymatic hydrolysis of these glycoconjugates are performed by wine microorganisms. Thus, the liberation of the odorous aglycon is achieved by the action of the β-D-glucosidase enzyme, being necessary for diglycosides prior to the activity of an appropriate exo-glycosidase [30]. According to Grimaldi et al. [31], O. oeni strains possess β-D-glucopyranosidase, α-D-glucopyranosidase, and β-D-xylopyranosidase activities but also minimal α-L-rhamnopyranosidase and α-L-arabinofuranosidase activities. Lactobacillus spp. and Pediococcus spp. also possess varying degrees of β-D-glucopyranosidase and α-D-glucopyranosidase activities, although approximately one order of magnitude less than those seen for O. oeni.
Although the β-glucosidase activity is strain dependent, it is present in all species capable to perform MLF. Numerous works have shown the ability of many Oenococcus oeni strains to hydrolyse grape glycoconjugate aroma precursors with differences in the extent and specificity of β-glucosidase activity [31][32][33][34]. The variability observed in different strains is a consequence of the influence of pH, sugar, and ethanol content of wine on β-glucosidase activity [32].
Lactiplantibacillus plantarum [35] (formerly Lactobacillus plantarum) strains isolated from South African wines [36] and Italian wines [37] showed β-glucosidase activity and the ability to release odorant aglycones from odourless glycosidic aroma precursors. Due to a more diverse enzyme profile observed in Lactiplantibacillus plantarum when compared with O. oeni strains, particularly with regards to the presence of the aroma-modifying enzymes β-glucosidase and phenolic acid decarboxylase (PAD), Krieger-Weber et al. [38] suggest and recommend the future use of this species in the modification of wine aroma profile and use as a commercial starter culture.
However, it is important to point out that, sometimes, glycosidase activity can also damage the final product quality by the increase in smoke taint-associated aromas [39][40] when some volatile phenols are the glycoconjugate compounds, or impacting wine colour when anthocyanin glucosides are involved [40].
Esterase-EC 3.1.1.6 acetyl ester hydrolases (Esterase activity)—Wine esters are secondary or tertiary aroma compounds that contribute significantly to wine aroma [40][41]. These compounds are produced by yeasts during alcoholic fermentation and by LAB during MLF [41] via ester hydrolysis through esterase activity and also by slow chemical esterification [41] between alcohol and acids during wine aging [42]. The main esters in wine include ethyl esters of organic acids (e.g., ethyl lactate), fatty acids (e.g., ethyl hexanoate, ethyl octanoate, ethyl decanoate), and acetates of higher alcohols (e.g., ethyl acetate, isoamyl acetate) [41]. There are many references to the role of LAB in the ester composition profile of wines after MLF produced worldwide [43][44][45][46]. Although all wine LAB species of Lactobacillus, Pediococcus, and Oenococcus possess esterase activity, strains of O. oeni have shown the highest activity [47]. The degree of LAB contribution to the ester profile of the wine is strain-specific [28][48] and is conditioned by factors such as pH, temperature, and ethanol concentration [47]. Sumby et al. [28] realized that O. oeni esterases can hydrolyse and also synthesise esters of short-chained fatty acids, the degree of each activity being conditioned by strain and by wine composition. Additionally, according to Lasik-Kurdy et al. [49] results, the MLF inoculation strategy can affect the quantity and quality of esters released by the bacteria, with the co-inoculation technique showing an increase in the release of ethyl esters (ethyl lactate, diethyl succinate, and ethyl acetate), that may enhance the wine with floral and fruity notes, depending on their concentration.
Lipase-EC 3.1.1.3 triacylglycerol acylhydrolases (Lipase activity)—By their action, wine lipids are cleaved, rendering different volatile compounds (esters, ketones, aldehydes) and fatty acids. While the former may have a positive effect on wine flavour, the odours of fatty acids are usually not desirable [50]. Lipase activities are present in all genera of wine LAB. In a survey performed by Matthews et al. [51] in LAB isolated from Australian wines, for enzymes of interest in oenology, lipase activity was restricted to three Lactobacillus isolates. From palm wine, Nkemnaso [52] recovered six LAB isolates—Lactiplantibacillus plantarum, Lactiplantibacillus pentosus, Levilactobacillus brevis, Limosilactobacillus fermentum [35], formerly Lactobacillus plantarum, Lactobacillus pentosus, Lactobacillus brevis, Lactobacillus fermentum-, Lactococcus spp., and Leuconostoc spp.) with lipase activity.
Proteases and peptidases (Proteolytic activity)—Although, having complex nutritional requirements, O. oeni and other wine LAB strains belonging to other species responsible for MLF cannot utilize inorganic nitrogen sources, contrary to the fermentation yeast Saccharomyces cerevisiae. Instead, sufficient amounts of organic nitrogen in the form of amino acids and peptides must be supplied or be present in musts or wines [38]. Thus, some works have characterised proteolytic enzymes in O. oeni strains [53][54][55][56] and in wine Lactobacillus strains [57] that may help to gain access to rare nitrogen sources during MLF [56]. According to the results obtained by Aredes Fernández et al. [5], the utilisation of Oenococcus oeni with proteolytic activity to carry out the MLF would contribute to enhancing the beneficial biological activities (antioxidant and antihypertensive activity) of the final product and provide an additional value to regional wines. Wine LAB proteolytic activities could be exploited in winemaking and have the potential to replace or reduce the use of fining agents such as bentonite for the removal of unwanted wine proteins [38].
Tannase-EC 3.1.1.20 (Tannase activity)—The activity of taninoacil hydrolase enzyme, commonly termed tannase, reduces wine astringency and turbidity and may increase the quality of wine and result in a better and pleasant sensory perception for consumers. This activity was observed in strains of Lactiplantibacillus plantarum [35] (formerly Lactobacillus plantarum) [5][58][59][60] and Limosilactobacillus frumenti [35] (formerly Lactobacillus frumenti) [59] Oenococcus oeni [50][61] and Pediococcus [51].
Other enzymes (Enzymatic activity)—Also very important is the ability of some LAB strains to produce enzymes that degrade biogenic amines (BAs) and mycotoxins. Aromatic amines such as tyramine, phenylethylamine, tryptamine, or serotonin are another class of compounds that can be oxidized by laccases [4][50]. Two laccases (multicopper oxidases) extracted from a wine strain Lactiplantibacillus plantarum J16 and a cereal strain Pediococcus acidilactici CECT 5930 were identified and characterized [62][63], revealing BA degradation. Additionally, Olmeda et al. [64] characterised Pediococcus laccases of P. acidilactici 5930 and Pediococcus pentosaceus 4816 strains. A Lactiplantibacillus plantarum strain (CAU 3823) was able to degrade biogenic amines in culture media conditions and Chinese rice wine at the end of post-fermentation [65]. The authors defend the approach of using strains such as this one as an efficient method to decrease the biogenic amine contents in traditional fermented food made by multiple microbes such as wine, rice wine, sausages, vinegar, cheese, and kimchi, among others.
Regarding detoxification activity, LAB are on the top of the list of microorganisms for the degradation of mycotoxins due to their GRAS status as mentioned before. For detoxification of mycotoxins in foods, LAB may use two mechanisms: (i) using the viable cell of the microorganisms and/or (ii) using the enzymes produced by certain LAB strains [66]. In a group of LAB isolated from Douro wines and identified as belonging to O. oeni, Lactobacillus plantarum, Pediococcus parvulus, Abrunhosa et al. [67] detected biodegradation of ochratoxin A (OTA) in a synthetic medium only in Pediococcus parvulus strains able to degrade OTA. Due to the OTA degradation ability of these strains, potential biotechnological applications to reduce health hazards associated with this mycotoxin may be exploited not only in the wine industry but also in other food industries (sausage, beer) and feedstuff for animals [68].

4. Enzymes from Grapes and Commercial Preparations Used in Wines Production

In wine production, enzymes are required for the biotransformation processes that convert grape juice into wine. These processes are performed by enzymes from microorganisms (yeasts, fungi, bacteria) and grapes but also by commercial enzymatic preparations added exogenously [3][69].
Thus, enzymes can be used throughout the winemaking process. Their use improves the extraction of anthocyanins from the red berry skins, thereby increasing the colour intensity of the resulting wine, which is an important quality parameter in red wines. At this stage, commercial enzyme preparations are mainly characterised by the activities of pectolytic enzymes, namely polygalacturonase, pectin methylesterase, pectin lyase, cellulases, hemicellulases, and acid proteases [70][71].
Pectinases, xylanases, glucanases, and proteases are used to improve clarification and filtration. These enzymes can increase pressing efficiency and juice extraction [72]. The rupture of grape-cell structures by these enzymes favours the extraction of substances contained in the pulp and in the skin, improving the extraction and clarification processes of the grape must, while also extracting substances that impact the aroma and colour of the final wine [4][72].
Once the alcoholic fermentation finishes, contact with lees takes place. Wine lees are defined as ‘the residue that forms at the bottom of the vessel containing wine after alcoholic fermentation during the storage or after authorised treatments, as well as the residue obtained following the filtration or centrifugation of this product in accordance with EEC regulation No. 337/79. Lees are mainly composed of dead yeasts and bacteria, tartaric acid, and inorganic matter [73]. Yeast autolysis occurring after cell death involves the hydrolysis of biopolymers under the action of hydrolytic enzymes such as β-glucanases and proteases, releasing peptides, amino acids, fatty acids, and nucleotides from the yeast cytoplasm to the wine. Glucans and mannoproteins from the yeast’s cell wall are also released and influence significantly the stability and the final sensory properties of the wines. Aiming at reducing the wine’s contact with lees and preventing the risks of oxidation and microbial contamination, enzymatic preparations rich in β-glucanases can be used. Exogenous glucanases can catalyse the hydrolysis of β-(1-3) and β-(1-6)-glycosidic bonds of the cell wall β-glucan chains, progressively degrading the cell wall and accelerating the yeast lysis [73][74].
Other enzymes may be used with the aim of improving wine varietal aroma by releasing glycosidic aroma precursors that are stable during winemaking operations since the glycosidases activity of S. cerevisiae is somewhat limited [75]. Commercial enzymatic preparations, rich in glycosidases, are available from Aspergillus niger and can be used in winemaking [76].
Commercial enzyme preparations usually consist of blends of different activities—glucosidases, glucanases, pectinases, and proteases [77]—and the quest for enzymes with more specific characteristics will continue. One major goal of the current research is to study the high endogenous enzyme potential of wine microorganisms.
Under the pH values and sulphur dioxide concentrations typically found in the winemaking process, grape enzymes are often poorly active [78]. Therefore, commercial enzymatic preparations are applied at different stages of the winemaking process for several purposes (lowering viscosity and increasing juice yield, enhancing colour extraction, releasing varietal aromas from precursor compounds, improving the clarification and filterability, and reducing ethyl carbamate formation, among others) as they present a better tolerance and, consequently, activity in the winemaking condition [68][79][80]. The commercial enzymatic preparations from a fungal origin [produced especially by Aspergillus spp. are accepted as GRAS (Generally Recognised as Safe), except glucanases that are produced by direct fermentation—for example, of Trichoderma harzianum, Trichoderma longibrachiatum (T. reesei) and Penicillium funiculosum, Lactobacillus fermentum for urease (EC 3.5.1.5) and hen egg white for Lysozyme], are pectinases, hemicellulases (EC 3.2.1.7 8), β-glucanases (EC 3.2.1.5 8), xylanases, and glycosidases (EC 3.2.1.2 0) that are included in the International Code for Oenological Practices of the International Organisation of Vine and Wine [81]. In addition, Arabinanases (EC 3.2.1.9 9), Cellulases (EC 3.2.1.4), Glucosidases (EC 3.2.1.2 1), Galactanases (EC 3.2.1.8 9), Pectinlyases (EC 4.2.2.1 0), Pectinmethylesterases (EC 3.1.1.1 1) and Polygalacturonases (EC 3.2.1.1 5) are included in International Code for Oenological Practices of the International Organisation of Vine and Wine [81].

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Subjects: Biotechnology & Applied Microbiology
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Fernanda Cosme
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