CA1213772A - Process for the preparation of a functional bioprotein, the bioprotein thus obtained and preparations containing it - Google Patents
Process for the preparation of a functional bioprotein, the bioprotein thus obtained and preparations containing itInfo
- Publication number
- CA1213772A CA1213772A CA000444377A CA444377A CA1213772A CA 1213772 A CA1213772 A CA 1213772A CA 000444377 A CA000444377 A CA 000444377A CA 444377 A CA444377 A CA 444377A CA 1213772 A CA1213772 A CA 1213772A
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- Prior art keywords
- bioprotein
- functional
- protein
- hydrolysis
- cheese
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Classifications
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/347—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of proteins from microorganisms or unicellular algae
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C19/00—Cheese; Cheese preparations; Making thereof
- A23C19/06—Treating cheese curd after whey separation; Products obtained thereby
- A23C19/068—Particular types of cheese
- A23C19/08—Process cheese preparations; Making thereof, e.g. melting, emulsifying, sterilizing
- A23C19/082—Adding substances to the curd before or during melting; Melting salts
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C19/00—Cheese; Cheese preparations; Making thereof
- A23C19/06—Treating cheese curd after whey separation; Products obtained thereby
- A23C19/09—Other cheese preparations; Mixtures of cheese with other foodstuffs
- A23C19/093—Addition of non-milk fats or non-milk proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L25/00—Food consisting mainly of nutmeat or seeds; Preparation or treatment thereof
- A23L25/10—Peanut butter
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/195—Proteins from microorganisms
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Mycology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- General Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Cell Biology (AREA)
- Molecular Biology (AREA)
- Dairy Products (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Grain Derivatives (AREA)
Abstract
Abstract of the disclosure:
Functional bioproteins are obtained from micro-bial protein isolates by extraction of a microbial pro-tein to decrease its content of nucleic acids and lipids, followed by enzymatic hydrolysis with physiologic endo-proteases under mild conditions. The products are suit-able as protein components in high-protein foodstuffs, such as cheese-like products, coffee whiteners or spreads.
Functional bioproteins are obtained from micro-bial protein isolates by extraction of a microbial pro-tein to decrease its content of nucleic acids and lipids, followed by enzymatic hydrolysis with physiologic endo-proteases under mild conditions. The products are suit-able as protein components in high-protein foodstuffs, such as cheese-like products, coffee whiteners or spreads.
Description
It has already been proposed that functionaL
hydrolysates of microbial protein ;solates be prepared by initially subject;ng a m;crob;al protein to an extrac-t;on treatment to reduce the content of nucleic acids and l;p;ds in it, and then subjecting it to enzymatic hydro-lysis by one or more endoproteases (Canadl~n Patent Application No. 414,860).The protein hydrolysates have advantageous properties in the technoLogy of foodstuffs and bring about not only a nutritional improvelnent in foods, but also facilitate the ;ndustrial processing of them, especially if they have a porous structure but, at the same time, contain ~ater-soluble and lipid~soluble constituents, as is the case ~ith desserts, baked pro-ducts and pasta, and imitation cheeses~ One fraction of these protein hydrolysates shows a particularly high emulsifiability as is required for sausage products~
cheese products, confect;onery and creams~ but aLso for mayonnaise and salad sauces or other fat preparations.
It has no~ been found that spec;fic protein hydrolysates of this type are able to serve not only as food additives contained in foodstuffs to only a minor extent, but rather as protein components ;n hi~h-protein foodstuffs~ especially ;n cheese-like products.
The invenLion relates to 3 process for the pre-paration of a functionaL hydroLysate of microbial protein ~ 3 isolates by extraction of a micrchial protein to decrease its content of nucleic acids and lipids~ follo~led by enzym-atic hydrolysis by endoproteases, which process comprises carrying out the hydrolysis with physiologic proteases under mild cond;tionsf and relates to the functiol7al protein hydro-lysate-s obtainable thus and to preparations which contain these functional prote-in hydrolysates~ Preferred embodi-ments of the invention are illustrated in more detail below.
All h-igh-protein microb;al cell aggregates are suitable as the startin~ material. The bacteriaL cell aggregates whicli are obtained according to Gerrnan Patent
hydrolysates of microbial protein ;solates be prepared by initially subject;ng a m;crob;al protein to an extrac-t;on treatment to reduce the content of nucleic acids and l;p;ds in it, and then subjecting it to enzymatic hydro-lysis by one or more endoproteases (Canadl~n Patent Application No. 414,860).The protein hydrolysates have advantageous properties in the technoLogy of foodstuffs and bring about not only a nutritional improvelnent in foods, but also facilitate the ;ndustrial processing of them, especially if they have a porous structure but, at the same time, contain ~ater-soluble and lipid~soluble constituents, as is the case ~ith desserts, baked pro-ducts and pasta, and imitation cheeses~ One fraction of these protein hydrolysates shows a particularly high emulsifiability as is required for sausage products~
cheese products, confect;onery and creams~ but aLso for mayonnaise and salad sauces or other fat preparations.
It has no~ been found that spec;fic protein hydrolysates of this type are able to serve not only as food additives contained in foodstuffs to only a minor extent, but rather as protein components ;n hi~h-protein foodstuffs~ especially ;n cheese-like products.
The invenLion relates to 3 process for the pre-paration of a functionaL hydroLysate of microbial protein ~ 3 isolates by extraction of a micrchial protein to decrease its content of nucleic acids and lipids~ follo~led by enzym-atic hydrolysis by endoproteases, which process comprises carrying out the hydrolysis with physiologic proteases under mild cond;tionsf and relates to the functiol7al protein hydro-lysate-s obtainable thus and to preparations which contain these functional prote-in hydrolysates~ Preferred embodi-ments of the invention are illustrated in more detail below.
All h-igh-protein microb;al cell aggregates are suitable as the startin~ material. The bacteriaL cell aggregates whicli are obtained according to Gerrnan Patent
2,633,451 by culturing bacteria of the strain Methylomonas clara ATCC ~1226 in a nutr;ent medium containin0 methanol, out of which acigre-~ates the lipicls have essentially been rcmoved by the process in German Auslegeschrift 2,h33~6~6, by extrac-tiorl with a mixture, which is larciely or completely anhydrous, of ammonia and a polar solvent from the series of lower alkanols; lo~ler glycols or methyl or ethyl ethers of a lo~er glycol, in particular nethanol, and the nucle;c ac;ds llave essentially been removecl in a subsequellt step by extraction uith water~r are particularly advant-ageous.
Trypsin~ chymotrypsin and mixtures thereof are pre-ferred as the physiologic endoproteasesr Trypsin is particularly preferred. These endoproteases lead to a product havil~g a satisfac10ry flavor and valuable phys;o--logic and industrial propert1es. It is possible to use "aggressivc" en~yl,lesr hut this requ-ires the main-ten~nce and r,icnitcring oF particularlv adjuste~ cond;~
r~ ~ e ~ 4 ~
tions, this not bcing generally advantageous by reason of the increased elaboration. Enzymes such as pepsin hich cleave in a very acid range lead, when neutral;zed as is subsequently necessary, to production of an inc-reased amount of salts which can be disadvantageousO
- Obv10llsly, the hydrolysis conditions are governed by the enzyme employed. In the case of the preferred proteases~ hydrolysis takes place in the ptl range 7 to 8, in particular at pH 7.5, in a ternperature range from ~0 10 to 50, in particular 45, C, over the course of 5 to 30, in particular about 20, minutes~ In general, 500 to 2,000 parts by weight, in particular about 1~0L10 parts by we;~ht, of substrate are employed per ont part by weight of protease.
When the hydrolysis has reached the required extent, the reaction is stopped, advan.ageously by inactivating the enzynle. This ;s advantageously carr;ed out by heating the batch to 70 to 90, ;n part;cular 80, C wh;ch takes a few M;r~utes.
The funct;onal protein thus obtained can be dried~ for example in a spray dryer, and it can then be stored. Whtn this dried material is used~ it is first resolvatized, this advantageously taking place under slit~ht vacuu~ in order to prevent inclusions of air~
However, it is advarltc1geous to process the pro-tein hydrolysate d;rectly to give the applopriate pre--paration~ Thus~ the hydrolysis can be carried out, for exampief in a processed cileese kettle after which tht product is ir~mediately further processed with the cus-i ~cooker) ~Z~77~ .
~ 5 tomary adclitives~ such as emulsifyin~ salts~
A number o-f processes~ in which the proportion of cheese used in processe~ cheese and simllar products is wholly or partly replaced by proteins wh;ch are more 5 readily manipulated industrially and are nlore -favorably pr;ced-, have already been disclosed. ~xamples of this are unriperled milk protein (Britisl1 Patent 1,601~672, German Offenlegungsschrift 2~834,093), caseinate (German Offenlegungsschrift 2,4-11,913, U.S. Patent ~,2~2,050) or products from whey (U~S. Patent 4,166,1(~2), some o~ them being used a~ter mixing with vegetable products, such as wheat gluten (U.S~ Patent 3~806,606),. soybean protein tlJ.S. Patent 4,080,477) or peanut prote-in (I:ood Techno-Lo~y, July 1979, 88 - 93).
The use of a microbial prote;n, a sodiurn, calciuln or magnesium salt, an acetylation product or a phosphate complex thereof or a l~eat-denatured microbial protein as the protein comporlent in foods, such as baked products, meat products, drinks, -fermented dairy substit;ute pro-ducts or desserts has been disclosed in German Offen-le~un~sschriFt 2,651,464.
It is important, ~or health and flavor reasons~
especially with protein isolates from bacteria, to decrease the cor~ent of nucleic acids and lipids. How-ever~ ~from the industrial v1ewpo-,nt, isolates of this type cannot directly be employed for ,oodstuffs~
If it is at.tempted, for example; to employ a protein isolate whicl1 ~as been prepclred by the Metl,od of German ~uslegeschrift 2~633,66S for a processed cheese like productt dif,iculties arise e~en when high propor tions of elnulsifying salts are usedr a homo~eneous and smooth emulsified composition is not obtained, and this is evident not only from the crurnbly and mealy cons;st-S ency, but it aLso leaves a gritty sensation like sar?cl inthe mouth.
t-lowevel, surprisingly, the fun~ctional bioprot2ins according to the invention ar excellently suitable as protein components for cheese substitute products. On 1U processing with customary emulsify1ng salts as ~re des-cribed in U.S. Patents 4,080,477 and 4,166,14Z, German Offenlegungsschriften 2,411,913 and 2,834,093 and British Patent 1,601,672~ ~ood protein breakdown, c~ood emulsifi-cation and a good texture are achieved, high-polymeric polyphosphates being preferred. P~eme1tabi1i-ty is achieved by mixtures of citrate and polyphosphate.
On manufacturin~ processed cheese-like products, it is possible to add othr protein carriers, such as cheese or the replacement products which have been men tioned. Butter fat and vegetable fats are suitable as the fat component. It is possible to add, in a customary manner, water an(3 auxiliaries, such as emlllsi~iers~
colorants and flavorings.
The products can be procssed in cuscolTIary Z5 machines (for exarnple pan, cutter or 1aydolln cooker) and filled out ;n a custor(lclry manner and packed, for example for spread;ng, ;n alu-m;num foil~ tubes, tubular film, jars or plastic tubs or, for slicing~ in blocks~ It is also poss;ble to
Trypsin~ chymotrypsin and mixtures thereof are pre-ferred as the physiologic endoproteasesr Trypsin is particularly preferred. These endoproteases lead to a product havil~g a satisfac10ry flavor and valuable phys;o--logic and industrial propert1es. It is possible to use "aggressivc" en~yl,lesr hut this requ-ires the main-ten~nce and r,icnitcring oF particularlv adjuste~ cond;~
r~ ~ e ~ 4 ~
tions, this not bcing generally advantageous by reason of the increased elaboration. Enzymes such as pepsin hich cleave in a very acid range lead, when neutral;zed as is subsequently necessary, to production of an inc-reased amount of salts which can be disadvantageousO
- Obv10llsly, the hydrolysis conditions are governed by the enzyme employed. In the case of the preferred proteases~ hydrolysis takes place in the ptl range 7 to 8, in particular at pH 7.5, in a ternperature range from ~0 10 to 50, in particular 45, C, over the course of 5 to 30, in particular about 20, minutes~ In general, 500 to 2,000 parts by weight, in particular about 1~0L10 parts by we;~ht, of substrate are employed per ont part by weight of protease.
When the hydrolysis has reached the required extent, the reaction is stopped, advan.ageously by inactivating the enzynle. This ;s advantageously carr;ed out by heating the batch to 70 to 90, ;n part;cular 80, C wh;ch takes a few M;r~utes.
The funct;onal protein thus obtained can be dried~ for example in a spray dryer, and it can then be stored. Whtn this dried material is used~ it is first resolvatized, this advantageously taking place under slit~ht vacuu~ in order to prevent inclusions of air~
However, it is advarltc1geous to process the pro-tein hydrolysate d;rectly to give the applopriate pre--paration~ Thus~ the hydrolysis can be carried out, for exampief in a processed cileese kettle after which tht product is ir~mediately further processed with the cus-i ~cooker) ~Z~77~ .
~ 5 tomary adclitives~ such as emulsifyin~ salts~
A number o-f processes~ in which the proportion of cheese used in processe~ cheese and simllar products is wholly or partly replaced by proteins wh;ch are more 5 readily manipulated industrially and are nlore -favorably pr;ced-, have already been disclosed. ~xamples of this are unriperled milk protein (Britisl1 Patent 1,601~672, German Offenlegungsschrift 2~834,093), caseinate (German Offenlegungsschrift 2,4-11,913, U.S. Patent ~,2~2,050) or products from whey (U~S. Patent 4,166,1(~2), some o~ them being used a~ter mixing with vegetable products, such as wheat gluten (U.S~ Patent 3~806,606),. soybean protein tlJ.S. Patent 4,080,477) or peanut prote-in (I:ood Techno-Lo~y, July 1979, 88 - 93).
The use of a microbial prote;n, a sodiurn, calciuln or magnesium salt, an acetylation product or a phosphate complex thereof or a l~eat-denatured microbial protein as the protein comporlent in foods, such as baked products, meat products, drinks, -fermented dairy substit;ute pro-ducts or desserts has been disclosed in German Offen-le~un~sschriFt 2,651,464.
It is important, ~or health and flavor reasons~
especially with protein isolates from bacteria, to decrease the cor~ent of nucleic acids and lipids. How-ever~ ~from the industrial v1ewpo-,nt, isolates of this type cannot directly be employed for ,oodstuffs~
If it is at.tempted, for example; to employ a protein isolate whicl1 ~as been prepclred by the Metl,od of German ~uslegeschrift 2~633,66S for a processed cheese like productt dif,iculties arise e~en when high propor tions of elnulsifying salts are usedr a homo~eneous and smooth emulsified composition is not obtained, and this is evident not only from the crurnbly and mealy cons;st-S ency, but it aLso leaves a gritty sensation like sar?cl inthe mouth.
t-lowevel, surprisingly, the fun~ctional bioprot2ins according to the invention ar excellently suitable as protein components for cheese substitute products. On 1U processing with customary emulsify1ng salts as ~re des-cribed in U.S. Patents 4,080,477 and 4,166,14Z, German Offenlegungsschriften 2,411,913 and 2,834,093 and British Patent 1,601,672~ ~ood protein breakdown, c~ood emulsifi-cation and a good texture are achieved, high-polymeric polyphosphates being preferred. P~eme1tabi1i-ty is achieved by mixtures of citrate and polyphosphate.
On manufacturin~ processed cheese-like products, it is possible to add othr protein carriers, such as cheese or the replacement products which have been men tioned. Butter fat and vegetable fats are suitable as the fat component. It is possible to add, in a customary manner, water an(3 auxiliaries, such as emlllsi~iers~
colorants and flavorings.
The products can be procssed in cuscolTIary Z5 machines (for exarnple pan, cutter or 1aydolln cooker) and filled out ;n a custor(lclry manner and packed, for example for spread;ng, ;n alu-m;num foil~ tubes, tubular film, jars or plastic tubs or, for slicing~ in blocks~ It is also poss;ble to
3'7~
endles s process them to produce slices in known~tuber bel~ or roller processes~
In addition, it is possibler using the ~-unc.^;Gnal bioproteins accordin~ to the invent;on, to manufacture other preparations, such as, for example~ spreads, coffee wllitcne*s, sauces or the like.
In the examples which follow~ ~percentage data relate to weight unless otherwise spec;fied. The addi-tives are characterized in compliance with the regula-tions ~overning the l;cens;ng of additives (ZZulV~ BGBl T.I r 1~81~ 1033).
*German E _ ple 1 Preparation of a functional bioprotein accordin~ to the i n v e n t :l o n .
The starting material used is a bacterial cell aggrc~ate according to German Patent 2,633,~S1, Cxample 2, the content in whicl1 o~ nucleic acids and lipids beirlg decrcased by the process in German Auslegeschrift 2~633,6O6, Example 1.
10 kg of this protein isolate are suspended in 65 liters of ~Jater and the pH of the suspension is adjusted to 7~5 by the addition of 4 N sodium hydroxide solution.
The suspension is preincubatecl at 45C with 25 stirring, tl1en 20 ~ or tryps-in PTN 3.0 S (supplied by ~ovo) are cadded and ;ncubat;on is carried out, wi'ch s-tirring, at 45~` for 20 min. To ;nacc'ivate the enzyme, the batch is heated to ~0C ~or 10 min arld the suspensiQn is spray-dried'. 1'he p~l o, the product falls to values 7~
. ~
hetween ~.5 and 7~0 because of the hyclrGly~cic activity of the enzyme~
e_2 Production of analogs of slices of processed cheese containin0 50% fat in dry matter, and 56~ dry matter. The following recipe is used:
15.000 kg of rennet casein 5.000 kg of spray~dried hydrolyzed bioprote;n lsolate accord;ng to Example 1 30.000 kg of butter 3.000 kg of sk;mmed mil~ powder 0.600 kg of sod;um chloride 1.350 kg of comnlercial emlllsify,ng salt m;xture baseci on sodium polyphosphates ~E 450C), socdiurn citrates ~E 331), potassium monophosphates tE 340), sodium diphosphates (E 450 a), sodium triphos phates ~E 450 b) and sodium rnonophosphates (E 339) O~OS0 kg of ci~ric acid 2U 0.200 kg of cheese colorant 32.nG0 kg o~ water~ includin~ condeilsate~
; h~c~le~st~
wh;ch is provided with a stirrer at 120 rprn~ is raised to 80C l~ithin 7 min.
The product thus produced ;s characterized by a rat;o of bioprote;n isolate to rennet casein o-r 1 : 3.
The sl;ces show good elastic properties and good toasting characteristics.
7~
Fxam~le 3 Example 2 is repeated with the modificat;on that 25.000 kg of hydrogenated vegetable fat is ernplo~ed in place of the 30O000 kg o-f butterr and the armount of ~ater is increased to 37.000 kg. A product havins the same prope~t;es is obtained.
Example 4 Production of a product as in Example 2, but using the f Q l lowi ng recipe:
9.750 kg of rennet casein 9.750 k9 of spray-dried hydrolyzed bioproteirl isolate accordiny to Exarnple 1 30.000 kg cf butter - 3.000 kg of skinlrned milk powcler 0.600 kg of sodium chloride 1~350 kg of emulsifyin~ salt (as in Exarrlple 2) 0.050 kg of citric acid 0.200 kg of cheese colorant 32.000 kg of water including condensate.
Z0 The heating is carr;ed out as described in Example 2a The product thus produced is character-ized by a ratio of bioprotein isolate to rennet case;n of 1 o 1.
The slices stlow good elastic properties ancl moderate to ~tood toast;ng characteristics.
25 Example S
ExaMple 4 ;s repeated wi-th the modification that 25~000 kg o-f hydrogella;ed ve3etable fat are employed in place of the ~n.ooo k~ of butter, the arlount of water being incre;ised to 37nOOO k~ A product tlaving t}l~ san;e 2~
properties as in Example ~t iS obtained.
Production of analogs of processed cheese for spreading, containing 40% fat in dry rnatter and 41%
dry matter. The following recipe is used:
3.000 kg of rennet casein 9.000 kg of spray-dried hydrolyzed bioprotein isolate according to Example 1 1 2 . 0 0 0 k 9 of butter 2.000 kg of skimmed milk powder 0.400 kg of sodium chloride 1.300 kg of commercial ernulsifying salt based on sodium polyphosphates (E 450c) 2.400 kg of precooked cheese 5 33.500 kg of water including condensater ~cheese The temperature in the~processing equipment, which is provided with a stirrer at 120 rpm, is raised to 92C
~ithin 15 min.
The product thus produced is characterized by a 20 ratio o-f bioprotein isolate to rennet casein of 3 : 1n The cooled melt has ~ood spreading character;s-t;cs and exllibits an acceptable cheese-like behavior in the mouth.
e 7 ~_ . .
Exanlple 6 is repeated with the modificat;on that 9.6 kg of hydrogenated vegetable fat are employed in place of the 12.000 kQ of butter, the arnount o-f water be;ng ;ncreased to 35 900 kg. A product ha~lin~ the sar~e properties as in Example 6 is obtainedn 7~
Exam~
Production of analogs of processed cheese for spreading, containing 60% fat in dry matter, and 47% dry matter. The following recipe is used:
3~000 kg of rennet casein 9.000 kg of spray-dried hydrolyzed b;oprotein isolate according to Example 1 Z.000 kg of skimrned milk powder 23.000 kg of butter 1.500 kg of ernulsifying salt (as in Example h) 3.600 kg of precooked cheese 37.000 kg of water incLuding condensate.
The heatir,g is carried out as described in Example 6.
The product thus produced is characterized by a ratio of bioprotein isolate to rennet casein of 3 : 1.
The cooled cheese has good spreading characteris-tics and exhibits a pleasant cheese-like behavior in the mouth.
_xample 9 When the process is carried out as in Example 8r but 22.400 k~J of hydrogenaced vegetable fat are employed in place of the Z~000 kg oi butter, and the amount of water is increased to 43.400 kg, then a product having the same properties as in Example ~,is o,btained.
Example 10 Production oF a high-protein spread with a peanut flavor containing 25% fat in dry Ina~cter, and -SS% dry matter.
The follol~ing recipe is used:
~..2~ 7'â~2J
6.000 kg of skimmed milk powder 6.000 kg of spray-dried hydroLyzed bioprotein is~late according to Example 1 O .400 kg of sugar 12.000 kg of peanut butter 0.430 ky of commercial emulslfyirlg salt mixture based on sodium polyphosphates ~E 450c), sod;um mono-phosphates (E 339), sodium diphosphates (E 450a) and sodium triphosphates (E 450b) 0.05 kg of carboxymethylcellulose (E 466) 49.000 kg of water ;ncluding condensate.
The heating is carried out as described in Example 6.
The cooled melt has a good cons;stency and, com-pared with peanut butter~ has good spreading characteris-tics even in the cold state. The product has a pleasantpeanut flavor.
Example 11 Production of a high-protein spread with a peanut flavor and contain;ng 45X fat in dry matter, and 44% dry matter. The following recipe ;s used:
3.000 kg of skimmed milk powder 3.000 kg of spray-dried hydrolyzed bioprote;n -isolate accordillg to Example 1 6.000 kg of butter 0.200 kg of suyar 6.000 kg of peanut butter 0.220 kg of emulsify;rlg salt (as in Exalnple 10) 0~020 kg o-f carhoxymethylcellulose (E 466) Z0.600 kg of water including conderlsaten t Heating is carr;ed out as described in EY~ample 6.
The cooled melt has a good consistency and, com-pared with peanut butter~ has good spreading characteris-tics even in the cold state. The procluct has a pleasant peanut -flavor.
Exampl~e 12 When the process is carr;ed out as in Example 11, but 4.800 kg of hydrogenated veyetable fat is used in place of the 6~000 kg of butter, and 21.800 kg ;s used in place of the 20.600 kg of ~later, then the properties of the product correspond to those of that in Example 11.
Exarnple 13 Production of a coffee whitener.
The following recipe is used:
800 g of water 70 g of vegetable fat 120 g of corn syrup 60 9 of spray-dried hydrolyzed bioprotein isola-te accord;ng to Example 1 0 8 g of phosphate stabilizer mixture consistin~ of potas~
sium rnonophosphates (E 34U), sodium polypllosphates (E 450c) and sodium monophosphates (E 339)~
The pl~osphate stab;l;zer m-ixture ;s d;ssolved in the water, and then the other constituents are added and the mixturc is heated, homogenized and spray-dried.
The product clistr;butes well 7n coffee and exhibits ~Jood wllitellinl3 properties.
endles s process them to produce slices in known~tuber bel~ or roller processes~
In addition, it is possibler using the ~-unc.^;Gnal bioproteins accordin~ to the invent;on, to manufacture other preparations, such as, for example~ spreads, coffee wllitcne*s, sauces or the like.
In the examples which follow~ ~percentage data relate to weight unless otherwise spec;fied. The addi-tives are characterized in compliance with the regula-tions ~overning the l;cens;ng of additives (ZZulV~ BGBl T.I r 1~81~ 1033).
*German E _ ple 1 Preparation of a functional bioprotein accordin~ to the i n v e n t :l o n .
The starting material used is a bacterial cell aggrc~ate according to German Patent 2,633,~S1, Cxample 2, the content in whicl1 o~ nucleic acids and lipids beirlg decrcased by the process in German Auslegeschrift 2~633,6O6, Example 1.
10 kg of this protein isolate are suspended in 65 liters of ~Jater and the pH of the suspension is adjusted to 7~5 by the addition of 4 N sodium hydroxide solution.
The suspension is preincubatecl at 45C with 25 stirring, tl1en 20 ~ or tryps-in PTN 3.0 S (supplied by ~ovo) are cadded and ;ncubat;on is carried out, wi'ch s-tirring, at 45~` for 20 min. To ;nacc'ivate the enzyme, the batch is heated to ~0C ~or 10 min arld the suspensiQn is spray-dried'. 1'he p~l o, the product falls to values 7~
. ~
hetween ~.5 and 7~0 because of the hyclrGly~cic activity of the enzyme~
e_2 Production of analogs of slices of processed cheese containin0 50% fat in dry matter, and 56~ dry matter. The following recipe is used:
15.000 kg of rennet casein 5.000 kg of spray~dried hydrolyzed bioprote;n lsolate accord;ng to Example 1 30.000 kg of butter 3.000 kg of sk;mmed mil~ powder 0.600 kg of sod;um chloride 1.350 kg of comnlercial emlllsify,ng salt m;xture baseci on sodium polyphosphates ~E 450C), socdiurn citrates ~E 331), potassium monophosphates tE 340), sodium diphosphates (E 450 a), sodium triphos phates ~E 450 b) and sodium rnonophosphates (E 339) O~OS0 kg of ci~ric acid 2U 0.200 kg of cheese colorant 32.nG0 kg o~ water~ includin~ condeilsate~
; h~c~le~st~
wh;ch is provided with a stirrer at 120 rprn~ is raised to 80C l~ithin 7 min.
The product thus produced ;s characterized by a rat;o of bioprote;n isolate to rennet casein o-r 1 : 3.
The sl;ces show good elastic properties and good toasting characteristics.
7~
Fxam~le 3 Example 2 is repeated with the modificat;on that 25.000 kg of hydrogenated vegetable fat is ernplo~ed in place of the 30O000 kg o-f butterr and the armount of ~ater is increased to 37.000 kg. A product havins the same prope~t;es is obtained.
Example 4 Production of a product as in Example 2, but using the f Q l lowi ng recipe:
9.750 kg of rennet casein 9.750 k9 of spray-dried hydrolyzed bioproteirl isolate accordiny to Exarnple 1 30.000 kg cf butter - 3.000 kg of skinlrned milk powcler 0.600 kg of sodium chloride 1~350 kg of emulsifyin~ salt (as in Exarrlple 2) 0.050 kg of citric acid 0.200 kg of cheese colorant 32.000 kg of water including condensate.
Z0 The heating is carr;ed out as described in Example 2a The product thus produced is character-ized by a ratio of bioprotein isolate to rennet case;n of 1 o 1.
The slices stlow good elastic properties ancl moderate to ~tood toast;ng characteristics.
25 Example S
ExaMple 4 ;s repeated wi-th the modification that 25~000 kg o-f hydrogella;ed ve3etable fat are employed in place of the ~n.ooo k~ of butter, the arlount of water being incre;ised to 37nOOO k~ A product tlaving t}l~ san;e 2~
properties as in Example ~t iS obtained.
Production of analogs of processed cheese for spreading, containing 40% fat in dry rnatter and 41%
dry matter. The following recipe is used:
3.000 kg of rennet casein 9.000 kg of spray-dried hydrolyzed bioprotein isolate according to Example 1 1 2 . 0 0 0 k 9 of butter 2.000 kg of skimmed milk powder 0.400 kg of sodium chloride 1.300 kg of commercial ernulsifying salt based on sodium polyphosphates (E 450c) 2.400 kg of precooked cheese 5 33.500 kg of water including condensater ~cheese The temperature in the~processing equipment, which is provided with a stirrer at 120 rpm, is raised to 92C
~ithin 15 min.
The product thus produced is characterized by a 20 ratio o-f bioprotein isolate to rennet casein of 3 : 1n The cooled melt has ~ood spreading character;s-t;cs and exllibits an acceptable cheese-like behavior in the mouth.
e 7 ~_ . .
Exanlple 6 is repeated with the modificat;on that 9.6 kg of hydrogenated vegetable fat are employed in place of the 12.000 kQ of butter, the arnount o-f water be;ng ;ncreased to 35 900 kg. A product ha~lin~ the sar~e properties as in Example 6 is obtainedn 7~
Exam~
Production of analogs of processed cheese for spreading, containing 60% fat in dry matter, and 47% dry matter. The following recipe is used:
3~000 kg of rennet casein 9.000 kg of spray-dried hydrolyzed b;oprotein isolate according to Example 1 Z.000 kg of skimrned milk powder 23.000 kg of butter 1.500 kg of ernulsifying salt (as in Example h) 3.600 kg of precooked cheese 37.000 kg of water incLuding condensate.
The heatir,g is carried out as described in Example 6.
The product thus produced is characterized by a ratio of bioprotein isolate to rennet casein of 3 : 1.
The cooled cheese has good spreading characteris-tics and exhibits a pleasant cheese-like behavior in the mouth.
_xample 9 When the process is carried out as in Example 8r but 22.400 k~J of hydrogenaced vegetable fat are employed in place of the Z~000 kg oi butter, and the amount of water is increased to 43.400 kg, then a product having the same properties as in Example ~,is o,btained.
Example 10 Production oF a high-protein spread with a peanut flavor containing 25% fat in dry Ina~cter, and -SS% dry matter.
The follol~ing recipe is used:
~..2~ 7'â~2J
6.000 kg of skimmed milk powder 6.000 kg of spray-dried hydroLyzed bioprotein is~late according to Example 1 O .400 kg of sugar 12.000 kg of peanut butter 0.430 ky of commercial emulslfyirlg salt mixture based on sodium polyphosphates ~E 450c), sod;um mono-phosphates (E 339), sodium diphosphates (E 450a) and sodium triphosphates (E 450b) 0.05 kg of carboxymethylcellulose (E 466) 49.000 kg of water ;ncluding condensate.
The heating is carried out as described in Example 6.
The cooled melt has a good cons;stency and, com-pared with peanut butter~ has good spreading characteris-tics even in the cold state. The product has a pleasantpeanut flavor.
Example 11 Production of a high-protein spread with a peanut flavor and contain;ng 45X fat in dry matter, and 44% dry matter. The following recipe ;s used:
3.000 kg of skimmed milk powder 3.000 kg of spray-dried hydrolyzed bioprote;n -isolate accordillg to Example 1 6.000 kg of butter 0.200 kg of suyar 6.000 kg of peanut butter 0.220 kg of emulsify;rlg salt (as in Exalnple 10) 0~020 kg o-f carhoxymethylcellulose (E 466) Z0.600 kg of water including conderlsaten t Heating is carr;ed out as described in EY~ample 6.
The cooled melt has a good consistency and, com-pared with peanut butter~ has good spreading characteris-tics even in the cold state. The procluct has a pleasant peanut -flavor.
Exampl~e 12 When the process is carr;ed out as in Example 11, but 4.800 kg of hydrogenated veyetable fat is used in place of the 6~000 kg of butter, and 21.800 kg ;s used in place of the 20.600 kg of ~later, then the properties of the product correspond to those of that in Example 11.
Exarnple 13 Production of a coffee whitener.
The following recipe is used:
800 g of water 70 g of vegetable fat 120 g of corn syrup 60 9 of spray-dried hydrolyzed bioprotein isola-te accord;ng to Example 1 0 8 g of phosphate stabilizer mixture consistin~ of potas~
sium rnonophosphates (E 34U), sodium polypllosphates (E 450c) and sodium monophosphates (E 339)~
The pl~osphate stab;l;zer m-ixture ;s d;ssolved in the water, and then the other constituents are added and the mixturc is heated, homogenized and spray-dried.
The product clistr;butes well 7n coffee and exhibits ~Jood wllitellinl3 properties.
Claims (10)
PROPERTY OF PRIVILEGE IS CLAIMED ARE DEFINED AS FOLLOWS:
1. A process for the preparation of a functional hydrolysate of microbial protein isolates by extraction of a microbial protein to decrease its content of nucleic acids and lipids, followed by enzymatic hydrolysis by endoproteases, which process comprises carrying out the hydrolysis with physiologic proteases under mild condi-tions.
2. The process as claimed in claim 1, wherein tryp-sin, chymotrypsin or mixtures thereof are employed as the endoprotease.
3. The process as claimed in claim 1, wherein trypsin is employed as the endoprotease.
4. The process as claimed in one or more of claims 1 to 3, wherein the hydrolysis is carried out in the pH
range 7 to 8.
range 7 to 8.
5. The process as claimed in one or more of claims 1 to 3, wherein the hydrolysis is carried out in a tem-perature range from 40 to 50°C.
6. The process as claimed in one or more of claims 1 to 3, wherein the hydrolysis lasts 5 to 30 minutes.
7. A functional bioprotein which may be obtained in accordance with claim 1.
8. A protein-containing preparation containing a functional bioprotein as claimed in claim 7.
9. A cheese-like product containing a functional bioprotein as claimed in claim 7.
10. A spread, coffeewhitner or sauce containing a functional bioprotein as claimed in claim 7.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19823248568 DE3248568A1 (en) | 1982-12-30 | 1982-12-30 | METHOD FOR PRODUCING A FUNCTIONAL BIOPROTEIN, THE BIOPROTEIN SO AVAILABLE AND PREPARATIONS CONTAINING THIS |
| DEP3248568.9 | 1982-12-30 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1213772A true CA1213772A (en) | 1986-11-12 |
Family
ID=6182112
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000444377A Expired CA1213772A (en) | 1982-12-30 | 1983-12-29 | Process for the preparation of a functional bioprotein, the bioprotein thus obtained and preparations containing it |
Country Status (8)
| Country | Link |
|---|---|
| EP (1) | EP0117312A1 (en) |
| JP (1) | JPS59173095A (en) |
| AU (1) | AU2296783A (en) |
| CA (1) | CA1213772A (en) |
| DE (1) | DE3248568A1 (en) |
| DK (1) | DK604783A (en) |
| ES (1) | ES528470A0 (en) |
| ZA (1) | ZA839684B (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH02167052A (en) * | 1988-06-17 | 1990-06-27 | Kanebo Ltd | Oral ingestible composition |
| US5024849A (en) * | 1990-05-01 | 1991-06-18 | Nestec S.A. | Liquid coffee whitener |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3143947A1 (en) * | 1981-11-05 | 1983-05-11 | Hoechst Ag, 6230 Frankfurt | "FUNCTIONAL PROTEIN HYDROLYSATE, METHOD FOR THE PRODUCTION THEREOF AND FOOD CONTAINING THIS PROTEIN HYDROLYSATE" |
-
1982
- 1982-12-30 DE DE19823248568 patent/DE3248568A1/en not_active Withdrawn
-
1983
- 1983-12-23 EP EP83113060A patent/EP0117312A1/en not_active Withdrawn
- 1983-12-27 JP JP58244992A patent/JPS59173095A/en active Pending
- 1983-12-28 ES ES528470A patent/ES528470A0/en active Granted
- 1983-12-29 DK DK604783A patent/DK604783A/en not_active Application Discontinuation
- 1983-12-29 AU AU22967/83A patent/AU2296783A/en not_active Abandoned
- 1983-12-29 CA CA000444377A patent/CA1213772A/en not_active Expired
- 1983-12-29 ZA ZA839684A patent/ZA839684B/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| DK604783D0 (en) | 1983-12-29 |
| ZA839684B (en) | 1984-08-29 |
| JPS59173095A (en) | 1984-09-29 |
| ES8407376A1 (en) | 1984-09-16 |
| AU2296783A (en) | 1984-07-05 |
| DK604783A (en) | 1984-07-01 |
| DE3248568A1 (en) | 1984-07-05 |
| EP0117312A1 (en) | 1984-09-05 |
| ES528470A0 (en) | 1984-09-16 |
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