MXPA00011778A - Production of hydrolysate seasoning - Google Patents
Production of hydrolysate seasoningInfo
- Publication number
- MXPA00011778A MXPA00011778A MXPA/A/2000/011778A MXPA00011778A MXPA00011778A MX PA00011778 A MXPA00011778 A MX PA00011778A MX PA00011778 A MXPA00011778 A MX PA00011778A MX PA00011778 A MXPA00011778 A MX PA00011778A
- Authority
- MX
- Mexico
- Prior art keywords
- protein
- enzyme
- hydrolysis
- substrate
- activities
- Prior art date
Links
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 4
- 239000000413 hydrolysate Substances 0.000 title abstract 3
- 235000011194 food seasoning agent Nutrition 0.000 title abstract 2
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 52
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 52
- 102000004190 Enzymes Human genes 0.000 claims abstract description 47
- 108090000790 Enzymes Proteins 0.000 claims abstract description 47
- 238000000034 method Methods 0.000 claims abstract description 37
- 239000000463 material Substances 0.000 claims abstract description 33
- 230000003301 hydrolyzing Effects 0.000 claims abstract description 32
- 239000000835 fiber Substances 0.000 claims abstract description 27
- 235000015067 sauces Nutrition 0.000 claims abstract description 14
- 239000007788 liquid Substances 0.000 claims abstract description 13
- 239000000843 powder Substances 0.000 claims abstract description 13
- 230000002797 proteolythic Effects 0.000 claims abstract description 13
- 239000003795 chemical substances by application Substances 0.000 claims abstract 2
- 235000018102 proteins Nutrition 0.000 claims description 51
- 229940088598 Enzyme Drugs 0.000 claims description 31
- 238000006460 hydrolysis reaction Methods 0.000 claims description 27
- 108010068370 Glutens Proteins 0.000 claims description 24
- 235000021312 gluten Nutrition 0.000 claims description 24
- 239000000758 substrate Substances 0.000 claims description 24
- 241000894006 Bacteria Species 0.000 claims description 23
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 17
- 235000005822 corn Nutrition 0.000 claims description 17
- 235000005824 corn Nutrition 0.000 claims description 17
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 claims description 17
- 239000004310 lactic acid Substances 0.000 claims description 17
- 235000014655 lactic acid Nutrition 0.000 claims description 17
- 229940110715 ENZYMES FOR TREATMENT OF WOUNDS AND ULCERS Drugs 0.000 claims description 15
- 238000000855 fermentation Methods 0.000 claims description 15
- 230000004151 fermentation Effects 0.000 claims description 15
- 108091005771 Peptidases Proteins 0.000 claims description 13
- 150000001720 carbohydrates Chemical class 0.000 claims description 11
- 150000003839 salts Chemical class 0.000 claims description 11
- 239000011780 sodium chloride Substances 0.000 claims description 11
- 235000021307 wheat Nutrition 0.000 claims description 11
- 238000011081 inoculation Methods 0.000 claims description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 10
- 102000035443 Peptidases Human genes 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 8
- 239000007787 solid Substances 0.000 claims description 7
- 239000000203 mixture Substances 0.000 claims description 5
- 235000013311 vegetables Nutrition 0.000 claims description 5
- 241000233866 Fungi Species 0.000 claims description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 4
- 240000006439 Aspergillus oryzae Species 0.000 claims description 3
- 235000002247 Aspergillus oryzae Nutrition 0.000 claims description 3
- 240000008042 Zea mays Species 0.000 claims description 3
- 238000003825 pressing Methods 0.000 claims description 3
- 241000131386 Aspergillus sojae Species 0.000 claims description 2
- 235000019749 Dry matter Nutrition 0.000 claims description 2
- 240000007842 Glycine max Species 0.000 claims description 2
- 235000010469 Glycine max Nutrition 0.000 claims description 2
- 240000007594 Oryza sativa Species 0.000 claims description 2
- 235000007164 Oryza sativa Nutrition 0.000 claims description 2
- 229940024999 Proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 claims description 2
- 235000009566 rice Nutrition 0.000 claims description 2
- 240000008529 Triticum aestivum Species 0.000 claims 2
- 238000001035 drying Methods 0.000 claims 1
- 239000000796 flavoring agent Substances 0.000 claims 1
- 235000013355 food flavoring agent Nutrition 0.000 claims 1
- 238000005899 aromatization reaction Methods 0.000 abstract 1
- 239000000047 product Substances 0.000 abstract 1
- 108010002430 hemicellulase Proteins 0.000 description 15
- 241000209149 Zea Species 0.000 description 14
- 241000186612 Lactobacillus sakei Species 0.000 description 11
- 229940020899 hematological Enzymes Drugs 0.000 description 10
- 235000019833 protease Nutrition 0.000 description 10
- 241000209140 Triticum Species 0.000 description 9
- 238000007792 addition Methods 0.000 description 8
- 235000014633 carbohydrates Nutrition 0.000 description 8
- 239000008187 granular material Substances 0.000 description 8
- 229960002989 Glutamic Acid Drugs 0.000 description 7
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 7
- 235000013922 glutamic acid Nutrition 0.000 description 7
- 239000004220 glutamic acid Substances 0.000 description 7
- 239000004365 Protease Substances 0.000 description 6
- 102000033147 ERVK-25 Human genes 0.000 description 5
- 229940059442 hemicellulase Drugs 0.000 description 5
- 102000009127 Glutaminase Human genes 0.000 description 4
- 108010073324 Glutaminase Proteins 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 210000004027 cells Anatomy 0.000 description 3
- 108010007119 flavourzyme Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 108060001513 CLASP Proteins 0.000 description 2
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-Acetylglucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 2
- 102100001558 OGA Human genes 0.000 description 2
- 238000009835 boiling Methods 0.000 description 2
- 108010089934 carbohydrase Proteins 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 235000013312 flour Nutrition 0.000 description 2
- 230000002538 fungal Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 108060003266 nagZ Proteins 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 230000001681 protective Effects 0.000 description 2
- 235000015099 wheat brans Nutrition 0.000 description 2
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 210000002421 Cell Wall Anatomy 0.000 description 1
- 229920002101 Chitin Polymers 0.000 description 1
- DJHJJVWPFGHIPH-OODMECLYSA-N Chitin Chemical compound O[C@@H]1C(NC(=O)C)[C@H](O)OC(CO)[C@H]1COC[C@H]1C(NC(C)=O)[C@@H](O)[C@H](COC[C@H]2C([C@@H](O)[C@H](O)C(CO)O2)NC(C)=O)C(CO)O1 DJHJJVWPFGHIPH-OODMECLYSA-N 0.000 description 1
- 108010022172 Chitinases Proteins 0.000 description 1
- 102000012286 Chitinases Human genes 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- RGHNJXZEOKUKBD-SQOUGZDYSA-M D-gluconate Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O RGHNJXZEOKUKBD-SQOUGZDYSA-M 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N D-sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- DLRVVLDZNNYCBX-LIZSDCNHSA-N Gentiobiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)O1 DLRVVLDZNNYCBX-LIZSDCNHSA-N 0.000 description 1
- 108010056771 Glucosidases Proteins 0.000 description 1
- 102000004366 Glucosidases Human genes 0.000 description 1
- 240000001929 Lactobacillus brevis Species 0.000 description 1
- 240000004403 Lactobacillus casei Species 0.000 description 1
- 241001134659 Lactobacillus curvatus Species 0.000 description 1
- 241000186684 Lactobacillus pentosus Species 0.000 description 1
- 240000006024 Lactobacillus plantarum Species 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- PNNNRSAQSRJVSB-BXKVDMCESA-N Rhamnose Chemical compound C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)C=O PNNNRSAQSRJVSB-BXKVDMCESA-N 0.000 description 1
- CZMRCDWAGMRECN-GDQSFJPYSA-N Sucrose Natural products O([C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](CO)O1)[C@@]1(CO)[C@H](O)[C@@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-GDQSFJPYSA-N 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N Trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- XQYXRKKDHYPACC-UHFFFAOYSA-N [N].O=C Chemical compound [N].O=C XQYXRKKDHYPACC-UHFFFAOYSA-N 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 239000011942 biocatalyst Substances 0.000 description 1
- 230000024881 catalytic activity Effects 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000010192 crystallographic characterization Methods 0.000 description 1
- 230000000593 degrading Effects 0.000 description 1
- 230000002255 enzymatic Effects 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- WSFSSNUMVMOOMR-UHFFFAOYSA-N formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 1
- 229940050410 gluconate Drugs 0.000 description 1
- 150000004676 glycans Polymers 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000002452 interceptive Effects 0.000 description 1
- 230000003834 intracellular Effects 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 102000004882 lipase Human genes 0.000 description 1
- 108090001060 lipase Proteins 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 230000000873 masking Effects 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 230000002906 microbiologic Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 150000004804 polysaccharides Polymers 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 210000004215 spores Anatomy 0.000 description 1
- 230000001954 sterilising Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 238000009423 ventilation Methods 0.000 description 1
- DLRVVLDZNNYCBX-ZZFZYMBESA-N β-melibiose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)O1 DLRVVLDZNNYCBX-ZZFZYMBESA-N 0.000 description 1
Abstract
A process for the production of a hydrolysate seasoning which comprises hydrolysing a protein containing material with enzymes which contain proteolytic activities and fiber hydrolysing activities. The hydrolysate may be used as a liquid sauce, a paste or as a dried powder as a base for an aromatization agent in culinary products.
Description
PROCESS TO PREPARE A HYDROLYZED DRESSING
FIELD OF THE INVENTION
The present invention relates to a process for preparing a hydrolyzed dressing. more particularly with the preparation of a hydrolyzed dressing by biological hydrolysis of a protein-containing material.
BACKGROUND OF THE INVENTION
In our co-pending document EP-A-0824873, we describe a process for the preparation of a dressing, comprising: preparing koj i fermented protein from a protein-containing material and a carbohydrate; and hydrolysing the fermented koj i protein at a temperature between 15 ° C and 60 ° C and a pH of 4.5 to 10 for a period of about 6 hours to 28 days; characterized in that the inoculation with a culture of lactic acid bacteria at an inoculation density of 103 to
107 cfu / g of fermented koj i protein is carried out "either in the fermented koji protein stage or in the hydrolysis stage.
The purpose of lactic acid bacteria is to inhibit the development of contaminating bacteria and to protect the koji from abnormal fermentation and putrefaction caused by such contaminating bacteria. Some lactic acid bacteria, for example, Lactobacillus sake (L. sake), produce peptidases and fiber hydrolyzing enzymes. API ZYM equipment has been used to detect enzymatic activities produced by lactic acid bacteria such as phosphatases, lipases, aminopeptidases (leucyl-, valil, cystil-), protease (chymotrypsin) and carbohydrases (galactosidase, glucosidase, N-acetyl- β-glucosaminidase). However, they do not produce glutaminase activity extracellularly. Among the carbohydrases that are produced, N-acetyl-β-glucosaminidase is a fiber hydrolyzing enzyme. The substrate of this enzyme, N-acetyl-β-glucosamine, is commonly found in chitin. In other words, these lactic acid bacteria produce chitinase capable of degrading the polysaccharide chains of the walls of fungal cells. When API 50 CHL is used for the characterization of these lactic acid bacteria, they have been shown to be capable of decomposing mannose, rhamnose, N-acetyl-β-glucosamine, melibiose, sucrose, trehalose, β-gentiobiose and gluconate. All of these are carbohydrates commonly found in the walls of plant cells. Among them, gluconase is also an enzyme that degrades the walls of fungal cells. These properties make the lactic acid bacteria a valuable source of proteolytic and fiber hydrolyzing enzymes in addition to their protective behavior. BRIEF DESCRIPTION OF THE INVENTION
We have found that, in the preparation of a hydrolyzed dressing, by hydrolyzing a substrate of protein containing material with enzymes containing proteolytic activities and fiber hydrolyzing activities, a surprising improvement in the organoleptic properties of the dressing is observed. This improvement can be obtained with or without the preparation of koji and / or in the presence or absence of lactic acid bacteria. Accordingly, the present invention provides a process for the preparation of a hydrolyzed dressing which comprises hydrolyzing a substrate of protein-containing material with enzymes containing proteolytic activities and fiber hydrolyzing activities.
DETAILED DESCRIPTION OF THE INVENTION
The protein-containing material substrate can be a vegetable protein material such as soybean, wheat germ, corn gluten, rice gluten, wheat gluten, etc., or it can be a fermented koji protein, prepared from the material containing protein and a carbohydrate, for example, by fermenting one or more protein-containing materials together with a carbohydrate with a culture of Aspergillus oryzae and / or Aspergillus sojae. The carbohydrate can be, for example, wheat flour, toasted wheat or wheat bran. When the material that contains protein is a gluten which will undergo a koji fermentation, it is advantageously used as a substrate in the form of granules, forming a dough, which comprises adding water to a dried gluten in an amount of 19 to 60% by weight based on the weight of the dough, granulating the dough and if necessary , add water to adjust the moisture content from 35 to 60% by weight, based on the weight of the granules before sterilizing the granules by steam treatment. The preparation of the granules as a substrate that supports the koji fermentation of the above raw materials and the koji fermentation conditions are described in our co-pending document SG-A-9800488-0. The protein-containing material is a substrate which may contain 30 to 100% protein, preferably 70 to 90% protein. If desired, the substrate of protein-containing material can be inoculated with a lactic acid bacterium for protective purposes. The lactic acid bacteria can be, for example, L. sake, L. brevis, L. casei, L. curvatus, L. pentosus, L. plantarum, L. pentosaceus. The source of the enzyme containing proteolytic activities can be microorganisms such as bacteria, fungi or yeasts, etc., for example the enzyme can be the enzyme produced during koji fermentation, the proteolytic enzymes produced by lactic acid bacteria used to inoculate the substrate of proteinaceous material, a technical proteolytic enzyme, or it can be a combination of two or more of these enzymes. The technical enzyme can be, for example, a protease, peptidase or glutaminase (for example Alcalase and Flavorzyme from Novo Nordisk, Glutaminese from Amano Pte Lte). Technical enzymes are generally enzymes that have been isolated and purified to remove interfering activities, which can be harmful to processing. The technical enzyme containing proteolytic activities can be added to the vegetable protein substrate before koj i fermentation or it can be added to the hydrolyzate. The source of the enzyme containing fiber hydrolyzing activities may be microorganisms such as bacteria, fungi or yeasts, etc., for example, it may be a small amount of fiber hydrolyzing enzyme produced during koji fermentation, the fiber hydrolyzing enzymes produced by the lactic acid bacteria used to inoculate the protein material substrate, a fiber hydrolyzing technical enzyme or it can be a combination of two or more of these sources. The fiber hydrolyzing technical enzyme can be, for example, Hemicellulase from Amano Pte Ltd, Celluclast from Novo Nordisk, or Depol 40L from Biocatalyst Pte Ltd. The enzyme containing fiber hydrolyzing activities can be added to the vegetable protein substrate before Koji fermentation, or can be added to the hydrolyzate. Among the protein substrates, corn gluten has the most significant improvement in hydrolysis yield using an enzyme that possesses fiber hydrolyzing enzyme activity. Corn gluten contains a high percentage of carbohydrates (16.5%) and fibers (5.7%). These complex carbohydrates form an intact membrane when corn protein is found inside. The masking effect of the carbohydrate network greatly affects the accessibility of corn protein by proteases or peptidases. To increase the accessibility of corn protein, it is therefore necessary to break down the carbohydrate membrane by fiber hydrolyzing enzymes. Although it is not desired to join any theory, for the koji system, it is considered that these fiber hydrolyzing enzymes hydrolyze the cell walls of the Aspergillus micelle in koji, which causes the release of intracellular peptidases and glutaminases of koj i within the liidrolizate . These peptidases and extracellular glutaminases are definitely more efficient, which leads to an increase in the nitrogen yields of formalin and glutamic acid. Hydrolysis of the substrate of protein-containing material can be carried out at a temperature of 2 ° to 65 ° C, and at a pH of 4.5 to 10, for a period of 6 hours to 28 days, for example, as described in EP 0640294 or in our co-pending patent applications EP-A-0829205, EP-A-0824873 or EP -A- 0913097, which are hereby incorporated by reference in their entirety. In the last two applications, an inoculation with a culture of a lactic acid bacterium at an inoculation density of 103 to 107 cfu / g of fermented koji protein is carried out, either in the fermented koji protein stage or in the hydrolysis stage. In the present invention, the inoculation into the substrate of protein-containing material with a culture of a lactic acid bacterium at an inoculation density of
- 103 to 109 cfu / g of protein-containing material can be carried out either in the fermented koj i protein stage or in the hydrolysis step. The hydrolysis is preferably carried out at a temperature between 15 ° C and 37 ° C for a period of 12 hours to 5 days, and more preferably at a temperature between 37 ° C and 55 ° C for a period of 8 hours. to 2 days. Advantageously, the hydrolysis is carried out at a pH of 4.5 to 7.5. The hydrolysis can be carried out in the absence or presence of a salt, and when the salt is present, the amount of the salt can be up to 100% by weight based on the weight of the protein material. After hydrolysis, the hydrolyzed protein material can be pressed to separate a liquid sauce from the solid residue. The liquid sauce is advantageously pasteurized, for example, at a temperature of 90 ° to 140 ° C for a period of 15 seconds to 30 minutes, and then filtered to provide a liquid dressing. If desired, salt may be added either before or after pressing or filtering, to provide a product having a salt content of 0-60% by weight, based on the weight of the dry matter. If desired, the liquid sauce can be formed into a powder, for example, by concentration, and then dried, for example, vacuum dried to a low moisture content and finally milled to a powder to provide a solid dressing.
EXAMPLES
The following examples further describe the present invention.
Example 1
Water is added directly to a mixture of (6.04 kg) corn gluten, (2.16 kg) wheat flour and (0.43 kg) wheat bran to obtain a moisture content of 45%. The mass that is formed is fed into a crusher to form cylindrical granules, each with a diameter of 4 mm and a length of 10 mm. Additional moisture is introduced into the granules so that the moisture content of the granules is 47% by weight.
The granules are heated to 100 ° C and maintained at the same temperature for 10 minutes and cooled to below 40 ° C. The cooled extrudates are mixed with a liquid suspension of 2.5 g of Aspergillus oryzae spore inoculum and 10 g of a L. sake culture at 109 cfu / g. The hemicellulase enzyme technique, Hemicellulase from Amano Pte Ltd (activity = 90,000 u / g) is added to a concentration of 0.43% by weight of the cooked extrudate. During the 42 hours of koji fermentation, the following temperature profiles are maintained for the culture bed:
0 -. 0 - 25 hours 30 ° C 25 - 42 hours 27 ° C
The koji is mixed at the 18th to 25th hour to ensure sufficient air flow through the culture bed for good ventilation. After koji fermentation, the matured koji is harvested. The hydrolysis is carried out in a hydrolysis tank by adding water to obtain a hydrolyzate with a total solid of 18% m / m. The hydrolysis is carried out at 35 ° C for 48 hours and the pH is kept constant at 6.0 with the addition of a 40% NaOH solution. The corn gluten hydrolyzate has a high glutamic acid content of 1.01% m / m. The hydrolyzed product is pressed to separate the corn gluten sauce from the solid residue. Salt is added at a concentration of 15% m / m before pressing. Corn gluten sauce is treated with heat at 90 ° C for 20 minutes. The liquid sauce was concentrated by evaporation. The concentrate obtained is dried in a vacuum oven and ground until pulverized. For organoleptic evaluation, 12.5 g of liquid sauce or 3.5 g of powder are diluted with 250 ml of boiling water. In both cases, a test team of 8 experienced tasters found that the product has a better body than the product without the addition of the hemicellulase enzyme to the cooked extrudates.
Example 2
A process similar to that of Example 1 is carried out, except that the hemicellulase enzyme is added to the hydrolyzate at a concentration of 0.25% by weight of the hydrolyzate during the hydrolysis instead of the cooked extrudates before the koj i fermentation. The corn gluten hydrolyzate produced in this way also has a high glutamic acid content of 0.97% m / m. For organoleptic evaluation, 12.5 g of liquid sauce or 3.5 g of powder are diluted with 250 ml of boiling water. In both cases, a test team of eight experienced tasters found that the product has a better body than a product without the addition of the hemicellulase enzyme.
Example 3
220 kg of water are heated up to 35 ° C in a reactor. 60 kg of powdered corn gluten are added to the water with stirring. 380 g of Flavourzyme protease enzyme 2.4L (from Novo Nordisk) are added to the hydrolyzate. A culture of L. sake is also inoculated in the hydrolyzate so that a count of 10 cfu / ml is obtained. The temperature and pH are controlled at 35 ° C and 6.0, respectively, for 48 hours. It was found that the product hydrolyzed in this way has a higher content of glutamic acid (0.4% m / m) compared to the product without the inoculation of L. sake (0.2% m / m). The hydrolyzate is further processed as in Example 1 to produce corn gluten sauce powder. A better microbiological quality is also obtained during the hydrolysis compared to the product without the inoculation of L. sake. A test team of eight experienced tasters found that the product has a better body than a product without the addition of L. sake.
Example 4
A procedure similar to the one in the example is carried out
3, except that 380 g of protease technique enzyme, Flavourzyme 2.4L (from Novo Nordisk) and 700 g of hemicellulase enzyme, Hemicellulase from Amano Pte Ltd (activity = 90,000 u / g) are added to the hydrolyzate at the time of hydrolysis. ). The hydrolyzed corn gluten product produced in this way has a high glutamic acid content of 0.83% m / m. A test team of eight experienced tasters found that the product has a better body than a product without the addition of the hemicellulase enzyme, that is, an even better body than the product of Example 3 due to the presence of hydrolyzing enzyme of additional fiber, hemicellulase, in addition to the derivative of L. sake.
Example 5
A similar procedure was carried out as in Example 1, except that koji was produced in base in wheat gluten, instead of corn gluten and the hemicellulase enzyme enzyme, Hemicellulase from Amano Pte Ltd (activity = 90,000 u) was added. / g), to the hydrolyzate at a concentration of 0.25% by weight of the hydrolyzate at the beginning of the hydrolysis. The wheat gluten powder, in a 7: 3 ratio to the wheat gluten koji, is added to the hydrolyzate during hydrolysis. The amount of water is adjusted so that the hydrolyzate has a total solids of 18% m / m.
It was found that the hydrolyzed product has higher glutamic acid (2.10% m / m) and formaldehyde nitrogen (0.95% m / m) compared to the product without the inoculation of the hemicellulase enzyme (1.76% m / m and 0.88% m / m, respectively). A test team of eight experienced tasters found that the product has a better body than a product without the addition of hemicellulase enzyme.
Example 6
A procedure similar to the one in the example is carried out
, except that the fiber hydrolyzing enzyme is not added, corn gluten powder is added in the hydrolyzate instead of wheat gluten powder, and the ratio of koji to the powder is 7: 3 instead of 3: 7, 380 g of the protease technique enzyme, Flavourzyme 2.4L (from Novo Nordisk) and 380 g of the protease technique enzyme, Alcalase 1.5L (from Novo Nordisk) are also added in the hydrolyzate at the start of the hydrolysis. The hydrolyzed product prepared in this way has a high glutamic acid content of 1.83% m / m.
A test team of eight experienced tasters found that the product has a better body than a product without the addition of L. sake as the source of the fiber hydrolyzing enzyme.
Example 7
A procedure similar to that of Example 1 was carried out, except that the culture of L. sake was suppressed. A test team of eight experienced tasters found that the product has a better body than a product without the addition of the hemicellulase enzyme.
Claims (23)
1. A process for the preparation of a hydrolyzed dressing, which comprises hydrolyzing a substrate of protein-containing material with enzymes containing proteolytic activities and fiber hydrolyzing activities.
2. The process as described in claim 1, wherein the substrate of protein-containing material is soybean, wheat germ, corn gluten, rice gluten or wheat gluten.
3. The process as described in claim 1, wherein the substrate of protein-containing material is koji of fermented protein prepared from the protein-containing material and a carbohydrate.
4. A process according to claim 3, wherein the fermented protein koj i is prepared by fermenting one or more protein-containing materials together with a carbohydrate with a culture of Aspergillus oryzae and / or Aspergillus sojae.
5. The process as described in claim 1, wherein the enzyme containing proteolytic activities is derived from bacteria, fungi or yeasts.
6. The process as described in claim 1, wherein the enzyme containing proteolytic activities is the enzyme produced during koji fermentation, the proteolytic enzymes produced by the lactic acid bacteria used to inoculate the substrate of protein material, a technical enzyme proteolytic, or a combination of two or more of these enzymes.
7. The process as described in claim 1, wherein the enzyme containing fiber hydrolyzing activities are derived from bacteria, fungi or yeast.
8. The process as described in claim 1, wherein the enzyme containing fiber hydrolyzing activities is a fiber hydrolyzing enzyme produced during koji fermentation, the fiber hydrolyzing enzymes produced by the lactic acid bacteria used to inoculate the substrate of protein material, a fiber hydrolyzing technical enzyme, or it can be a combination of two or more of these enzymes.
9. The process as described in claim 1, wherein the enzyme containing proteolytic activity is added to the vegetable protein substrate prior to koj i fermentation or to the hydrolyzate.
10. The process as described in claim 1, wherein the fiber hydrolyzing enzyme is added to the vegetable protein substrate prior to koj i fermentation or to the hydrolyzate.
11. The process as described in claim 1, wherein the hydrolysis of the substrate of protein-containing material is carried out at a temperature of 2 ° to 65 ° C, at a pH of 4.5 to 10 for a period of 6 hours at 28 days.
12. The process as described in claim 1, wherein a culture of a lactic acid bacterium is inoculated into the substrate of protein-containing material at an inoculation density of 103 to 109 cfu / g of protein-containing material either in the koji stage of fermented protein or hydrolysis stage.
13. The process as described in claim 1, wherein the hydrolysis is carried out at a temperature between 15 ° C and 37 ° C for a period of 12 hours to 5 days.
14. The process as described in claim 1, wherein the hydrolysis is carried out at a temperature between 37 ° C and 55 ° C for a period of 8 hours to 2 days.
15. The process as described in claim 1, wherein the hydrolysis is carried out at a pH of 4.5 to 7.5.
16. The process as described in claim 1, wherein the hydrolysis of proteinaceous material is carried out in the absence or presence of salt.
17. The process as described in claim 16, wherein when the salt is present, the amount is up to 100% by weight based on the weight of the protein material.
18. The process as described in claim 1, wherein, after hydrolysis, the hydrolyzed protein material is pressed to separate a liquid sauce from a solid residue.
19. The process as described in claim 18, wherein the liquid sauce is pasteurized at a temperature of 90 ° to 140 ° C for a period of 15 seconds to 30 minutes and then filtered to provide a liquid dressing.
20. The process as described in claim 19, wherein, when the salt is absent during hydrolysis, salt is added either before or after pressing to provide a product having a salt content of 0-60% by weight, based on the weight of the dry matter.
The process as described in claim 20, wherein the liquid sauce is made into a powder by concentration, then dried to a low moisture content and finally milled to a powder to provide a solid dressing.
22. A process for the preparation of a dry hydrolyzate for use as a base for a flavoring agent in culinary products, which comprises drying the paste obtained according to claim 21 at a residual water level of up to 2%.
23. A hydrolyzed dressing obtainable by a process as described in any of the preceding claims. SUMMARY A process for the production of a hydrolyzed dressing is described, which comprises hydrolyzing a material containing protein with enzymes which contain proteolytic activities and fiber hydrolyzing activities. The hydrolyzate can be used as a liquid sauce, as a paste or a dry powder as a base for an aromatizing agent in culinary products.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
SG9906087.3 | 1999-12-02 |
Publications (1)
Publication Number | Publication Date |
---|---|
MXPA00011778A true MXPA00011778A (en) | 2002-06-05 |
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