Enzymes developed and produced for industrial applications represent a market estimated at a global value comprised between $5000 million and $5500 million in 2016. The major applications for industrial enzymes include food and beverages (dairy, bakery, fruit juices, beer, wine), detergents, biofuel productions, animal feed, and other applications such as textiles, leather, and paper processing. Altogether, food and feed applications account for 55-60% of the global enzymes market, and market is still growing at an estimated 6-8% annual growth. The lipases category represents less than 10% of the global enzymes market, with a broad range of industrial applications: detergents, oil processing, food processing and pharmaceutical end-users. Existing applications and new development in the food and agroindustries sectors are reviewed. Keywords: industrial enzymes / enzyme producers / food / agroindustries / lipases / enzymes Résumé-Utilisation des lipases dans les agroindustries et les aliments. Les enzymes développées et produites pour les applications industrielles représentent un marché mondial dont la valeur est comprise entre $5000 millions et $5500 millions en 2016. Les principales applications industrielles des enzymes comprennent les applications agroalimentaires (produits laitiers, boulangerie, jus de fruits, bière, vin) et les applications non alimentaires telles que les détergents, la production de biocarburants, la nutrition animale ou encore les textiles, le cuir et l'industrie papetière. Globalement, les applications en nutrition humaine et animale représentent entre 55 % et 60 % du marché mondial des enzymes, avec une croissance annuelle estimée entre 6 % et 8 %. Les lipases représentent moins de 10 % du marché mondial des enzymes industrielles et sont utilisées dans de nombreux segments industriels tels que les détergents, la production des huiles et corps gras, les produits alimentaires et le secteur pharmaceutique. Cet article propose une revue d'applications actuelles et de développements récents dans les secteurs alimentaires et agroindustriels. Mots clés : industrielles / producteurs d'enzymes / industries agroalimentaires / agroindustries / lipases

SUMMARYAccumulation of water-soluble carbohydrates was studied in leaf tissues of 8-wk-old plants of perennial ryegrass {Lolium perenne L. var. Bravo). The roots and leaf bases were cooled to low temperatures to reduce sink activity while source activity was enhanced by continuous illumination of the shoots. This resulted in accumulation of fructans, flrst in sheaths, subsequently in expanding leaves, and finally in blades. Fructan concentration increased from 6 to 23 mg g"^ f. wt in sheaths, from 8 to 30 mg g~^ f. wt in expanding leaves and from 6 to only 17 mg g"^ f. wt in mature leaf blades. Increase in concentration of low-DP fructans preceded accumulation of high-DP fructans. Expanding leaves accumulated significantly more glucose and fructose than did mature leaf tissue. Leaf blades contained a higher concentration of sucrose than either leaf sheaths or expanding leaves. Expanding leaves exhibited the greatest activity of SST (0-77 nkat g"^ f. wt), the mature leaf blades the least (0-09 nkat g"^ f. wt), whilst that of mature leaf sheaths was intermediate (0-27 nkat g"^ f. wt). In each leaf tissue, invertase activity was higher than SST activity. Under conditions of fructan accumulation, SST activity increased threefold in mature leaf sheaths and 1-2-fold in expanding leaves. In mature leaf blades, however, the activity remained constant at a low level. Invertase activity never increased. Inhibitors of protein synthesis (cycloheximide) and of RNA metabolism (actinomycin D) prevented any increase of SST activity in leaf sheaths. The results are discussed in relation to fructan metabolism in leaf tissues of Lolium perenne.

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Previous work on Lolium perenne showed that sucrose : sucrose fructosyltransferase (SST) activity did not increase concomitantly with fructan synthesis in regrowing leaves or in mature leaf blades of plants that have been subjected to carbohydrate-accumulating conditions. This was contrary to the pattern of SST activity in roots and stubble. To obtain further insight into the fructan synthesizing activities and to explain this discrepancy, total fructosyltransferase activity (FT) was assayed by increasing the sucrose and the soluble enzyme concentrations and was compared to sedimentable phlein sucrase activity (PS) throughout the regrowth period following defoliation in leaves, stubble and roots. Before analysis on 2-month-old plants, PS activity was characterized in dark-grown coleoptiles, using [U-"%C]sucrose. PS activity had a pH optimum of 6n0 and produced 1-kestose in addition to high molecular weight fructans with a mean DP of 9. In 2-month-old plants, sedimentable PS and FT soluble reactions contained an initial sucrose concentration of 160 mM and 400 mM and proteins equivalent to 1n4 and 2n1 g f. wt of tissue, respectively. In stubble and roots, the FT preparation catalysed the synthesis of large fructans, and the overall pattern resembled the native fructans when separated by anion exchange HPLC. In regrowing leaves, the FT preparation produced low-DP fructans relatively more than in vivo but synthesized the high-DP fructan characteristic of the tissue. Moreover, FT activity did not remain at a low level like SST activity but increased from day 5 after defoliation when fructans began to accumulate. PS activity formed very few low-DP fructans and 1-kestose was the main product. Trisaccharides generated by PS activity represented 2-5% of the total trisaccharide synthesis. High-DP fructans were detectable only when the products of the reaction were concentrated 100 times. Results are discussed with respect to the relative contribution of FT and PS activities for the synthesis of 1-kestose and fructans in roots, stubble and leaves of Lolium perenne.

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