CN106867731A - The control method of proteinase A activity in beer production - Google Patents
The control method of proteinase A activity in beer production Download PDFInfo
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- CN106867731A CN106867731A CN201710195337.6A CN201710195337A CN106867731A CN 106867731 A CN106867731 A CN 106867731A CN 201710195337 A CN201710195337 A CN 201710195337A CN 106867731 A CN106867731 A CN 106867731A
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- 230000000694 effects Effects 0.000 title claims abstract description 47
- 238000000034 method Methods 0.000 title claims abstract description 42
- 235000013405 beer Nutrition 0.000 title claims abstract description 41
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 18
- 101001091368 Rattus norvegicus Glandular kallikrein-7, submandibular/renal Proteins 0.000 title claims abstract description 8
- 101000898773 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Saccharopepsin Proteins 0.000 title claims abstract description 8
- 102000004190 Enzymes Human genes 0.000 claims abstract description 62
- 108090000790 Enzymes Proteins 0.000 claims abstract description 62
- 235000014101 wine Nutrition 0.000 claims abstract description 49
- 239000007788 liquid Substances 0.000 claims abstract description 48
- 101710180012 Protease 7 Proteins 0.000 claims abstract description 37
- 238000012360 testing method Methods 0.000 claims abstract description 28
- 230000001954 sterilising effect Effects 0.000 claims abstract description 19
- 239000012530 fluid Substances 0.000 claims abstract description 17
- 238000000855 fermentation Methods 0.000 claims abstract description 16
- 230000004151 fermentation Effects 0.000 claims abstract description 16
- 238000004659 sterilization and disinfection Methods 0.000 claims abstract description 14
- CZMRCDWAGMRECN-UGDNZRGBSA-N 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 claims abstract description 11
- 229930006000 Sucrose Natural products 0.000 claims abstract description 11
- 239000005720 sucrose Substances 0.000 claims abstract description 11
- 238000002156 mixing Methods 0.000 claims abstract description 8
- 238000009928 pasteurization Methods 0.000 claims description 5
- 241000894006 Bacteria Species 0.000 claims description 2
- 238000005374 membrane filtration Methods 0.000 claims description 2
- 239000000706 filtrate Substances 0.000 claims 1
- 238000001914 filtration Methods 0.000 abstract description 17
- 108010051210 beta-Fructofuranosidase Proteins 0.000 abstract description 10
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 7
- 235000011073 invertase Nutrition 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 239000001573 invertase Substances 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 5
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 4
- 239000006260 foam Substances 0.000 description 4
- 230000009849 deactivation Effects 0.000 description 3
- 239000007850 fluorescent dye Substances 0.000 description 3
- UPSFMJHZUCSEHU-JYGUBCOQSA-N n-[(2s,3r,4r,5s,6r)-2-[(2r,3s,4r,5r,6s)-5-acetamido-4-hydroxy-2-(hydroxymethyl)-6-(4-methyl-2-oxochromen-7-yl)oxyoxan-3-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide Chemical compound CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@H]1[C@H](O)[C@@H](NC(C)=O)[C@H](OC=2C=C3OC(=O)C=C(C)C3=CC=2)O[C@@H]1CO UPSFMJHZUCSEHU-JYGUBCOQSA-N 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 240000000111 Saccharum officinarum Species 0.000 description 2
- 235000007201 Saccharum officinarum Nutrition 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 229910002092 carbon dioxide Inorganic materials 0.000 description 2
- 239000001569 carbon dioxide Substances 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 235000013399 edible fruits Nutrition 0.000 description 2
- 235000014103 egg white Nutrition 0.000 description 2
- 210000000969 egg white Anatomy 0.000 description 2
- 238000001952 enzyme assay Methods 0.000 description 2
- 230000035800 maturation Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000008092 positive effect Effects 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 238000012795 verification Methods 0.000 description 2
- 238000010792 warming Methods 0.000 description 2
- 101710184309 Probable sucrose-6-phosphate hydrolase Proteins 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 102400000472 Sucrase Human genes 0.000 description 1
- 101710112652 Sucrose-6-phosphate hydrolase Proteins 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000001471 micro-filtration Methods 0.000 description 1
- 239000013618 particulate matter Substances 0.000 description 1
- 235000013809 polyvinylpolypyrrolidone Nutrition 0.000 description 1
- 229920000523 polyvinylpolypyrrolidone Polymers 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12C—BEER; PREPARATION OF BEER BY FERMENTATION; PREPARATION OF MALT FOR MAKING BEER; PREPARATION OF HOPS FOR MAKING BEER
- C12C11/00—Fermentation processes for beer
- C12C11/11—Post fermentation treatments, e.g. carbonation, or concentration
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Food Science & Technology (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Enzymes And Modification Thereof (AREA)
- Distillation Of Fermentation Liquor, Processing Of Alcohols, Vinegar And Beer (AREA)
Abstract
The invention discloses a kind of control method of proteinase A activity in beer production, including：Obtain maturing fermentation liquid and carrying out conventional filtration operation, obtain zymotic fluid stoste；Partial fermentation liquid stoste is carried out into high-temperature instantaneous sterilization afterwards, wine liquid after the enzyme that obtains going out；Finally take wine liquid and zymotic fluid stoste after the enzyme that goes out to be blent, protease A enzyme activity≤10 unit/ml in sucrose inversion enzyme test peper positive test and wine liquid, is carried out filling after the completion of blending in control gained wine liquid.Protease A enzyme activity can as far as possible be removed using the method for the invention, while retain certain invertase enzyme activity, and the purpose of stable and consistent between batch in beer product production process is realized.
Description
Technical field
The present invention relates to the control method of proteinase A activity in beer production, belong to beer brewing technology field.
Background technology
Protease A is the principal element for influenceing beer particularly Foam Stability of Unpasteurized Beer.Wang De is good et al. by difference
The beer sample of protease A enzyme activity (0~60 unit/ml) is stored in 20 DEG C of four weeks, and beer sample is detected with fluorogenic substrate method
Product protease A enzyme activity, foam stability is detected with holding property of bubble method, is as a result shown, beer foam attenuation degree is initial with beer
Protease A enzyme activity negatively correlated (beer science and technology, 2004 the 5th phases, technical research, p11~15), the i.e. initial protease A enzyme of beer
Work is lower, and beer beer foam attenuation degree is smaller, and especially when protease A enzyme activity is more than 20 units/ml, this trend is more
Substantially.
The main method of current beer industry control beer product protease A enzyme activity includes：
(1) take measures to improve during yeast activity reduces the death rate, fermentation process and separate yeast as early as possible.Or these measures
Influenceed by zymotic fluid quality control, it is difficult to realize the stability per batch products residual protein enzyme A enzyme activity, otherwise it is not enough to egg
White enzyme A enzyme activity drops to sufficiently low level.
(2) it is filling to use the modes such as PU values pasteurization high.But also there are some researches show with the liter of hot bottle process temperature
Height, protease A and other enzyme systems in beer, vigor (Chen Xu etc., using fluorescence bottom all on a declining curve of such as invertase
The research of thing method detection draft beer protease A method, brewing science and technology, 2009 the 4th phases, p108~113).Temperature Treatment is to egg
White enzyme A and sucrose inversion enzyme activity produce similar influence, when protease A is inactivated, it is most likely that invertase also loses
Vigor, causes the indexs such as the feeling of freshness of beer product to be affected.Therefore, the method is not suitable for all category beer products
Production.
So far the protease A enzyme activity precise control scheme of a set of maturation is not yet found, had both been ensured all kinds of residual in beer product
Deposit enzyme activity and keep certain balance, and reduce the uncertain shadow to beer product protease A enzyme activity in production process as far as possible
Ring.
The content of the invention
The technical problem to be solved in the present invention is to provide a kind of control method of proteinase A activity in beer production,
Protease A enzyme activity can as far as possible be removed using the method, while retaining certain invertase enzyme activity, and beer is realized
In process of producing product between batch stable and consistent purpose.
The control method of proteinase A activity in beer production of the present invention, including following operation：Obtain ripe
Zymotic fluid simultaneously carries out conventional filtration operation, obtains zymotic fluid stoste；Partial fermentation liquid stoste is carried out into high-temperature instantaneous sterilization afterwards,
Obtain going out wine liquid after enzyme；Finally take wine liquid and zymotic fluid stoste after the enzyme that goes out to be blent, invertase in control gained wine liquid
Protease A enzyme activity≤10 unit/ml in test paper positive test and wine liquid, is carried out filling after the completion of blending.
In above-mentioned control method, maturing fermentation liquid is obtained using existing conventional techniques, grasped by existing conventional filtration again afterwards
Make that (step such as including diatomite filtering, PVPP filterings, dilution, film refined filtration, main purpose is to make wine liquid limpid, removes yeast, height
The impurity such as molecule protein, particulate matter, while being diluted with deoxygenated water by beer product aimed concn) filtered to obtain
Zymotic fluid stoste.
In above-mentioned control method, the technique of high-temperature instantaneous sterilization is same as the prior art, is typically with existing conventional
Thin plate heat exchanger realizes that, when sterilization is carried out, feed liquid is into Thin plate heat exchanger and reaches 76~80 DEG C in a short time, herein temperature
The lower sterilization of degree is cooled to 0~4 DEG C by Thin plate heat exchanger in a short time again after about 30~60 seconds.
In above-mentioned control method, when blending, sucrose inversion enzyme test peper positive test in gained wine liquid is preferably controlled
And protease A enzyme activity is 5~10 units/ml in wine liquid.As for the ratio blent then according to beer species and each manufacturer
Concrete condition determination, when production draft beer is carried out using the equipment of the applicant, takes wine liquid and zymotic fluid stoste after the enzyme that goes out
By 1:1~4:When 1 mass ratio is blent, above-mentioned level can be reached.
Consider from sanitation point, can also again carry out a bacteria removing before filling the container or after filling.When blending obtained wine thereby
Preferably make after filling during protease A enzyme activity >=5 unit/ml in sucrose inversion enzyme test peper positive test and wine liquid in liquid
Carried out with the pasteurization that PU values are 2~3 degerming；The temperature of sterilizing is now controlled to be no more than 55 DEG C.And work as and blend gained wine liquid
Protease A enzyme activity≤5 unit/ml in middle sucrose inversion enzyme test peper positive test and wine liquid, preferably before filling the container using micro-
Membrane filtration is degerming, and the selection of the microfiltration membranes is same as the prior art, usually 0.6 micron and 0.45 micron of filter membrane.
Compared with prior art, the method have the characteristics that：
1st, the present invention adjusts final wine liquid by way of wine liquid and zymotic fluid stoste are blent after using the enzyme that goes out
Enzyme activity, by protease A enzyme activity in wine liquid after the ratio of both control can be filtered with precise control；On the other hand make full use of existing
There is the instantaneous sterilization technology of maturation, enforcement difficulty is low, simple to operate, be capable of achieving Automated condtrol；
2nd, the present invention proposes, in filtering fermentation liquor stage control enzyme activity, aseptic filtration or low temperature bar to be used in the filling stage
Family name's process for sterilizing, recurrent blocking up stops phenomenon so as to cause tunnel type sterilization machine in process of production to be prevented effectively from existing process
Middle product excessive sterilization, the risk of invertase complete deactivation, are more beneficial for the control of production process quality stability.
Specific embodiment
With reference to specific embodiment, the present invention is described in further detail, to more fully understand present disclosure, but
The present invention is not limited to following examples.
To of the invention so that the applicant's unit different product and various processes formulate protease A control program as an example
Technical scheme is described further.
Embodiment 1
Draft beer is produced using the production line of the applicant, 180 days shelf-lifves, fermentation uses A yeast, A yeast suspensions
Property good, recovery time evening, need 10~12 days, be adapted to 12~14 DEG C of higher temperature fermentation, protease A dissolution is more.Producer
Case is as follows：
1st, ratio-dependent is blent：
Routinely technique obtains maturing fermentation liquid, collects 20 tank zymotic fluid data, including：
1) protease A Enzyme activity assay：Pure mellow wine detects protease A enzyme activity using fluorogenic substrate method after filtering, and average enzyme activity shows
Show 25.3 units/ml, fluctuation range is in 23~28 units/ml；
2) ratio primary election is blent：Relatively short for beer product in view of 180 day shelf-life, protease A enzyme is subjected to
Scope is 5~10 units/ml, and it is 2 that enzyme wine liquid of going out blends Proportionality design with stoste:1~4:1；
3) invertase enzyme activity verification：Take wine liquid after the normal filtration of part and be warming up to 80 DEG C and be incubated 10 minutes, it is ensured that sugarcane
Sugared invertase complete deactivation, test paper test is negative, and is cooled to 20 DEG C of normal temperature, and 2 are pressed respectively with stoste:1、3:1、4:1 blends 3 parts
Sample, carries out sucrose inversion enzyme test peper test again, and test result is shown as strong positive, strong positive, weakly positive；
Determine to blend ratio afterwards：Choose test result display strong positive and the maximum ratio of enzyme wine liquid accounting of going out, i.e., it is right
The Fruit variety 3:1 is most preferably to blend ratio；
2nd, pure mellow wine blends production, as a example by producing 100 tons of pure mellow wines：
Maturing fermentation liquid is filtered by existing routine operation, 25 tons of pure mellow wines of filtering enter target bright beer tank；Afterwards in warp
Instantaneous sterilization thin plate is accessed after conventional filtration flow, sterilization temperature is set and is set 74 DEG C, sterilizing time is set 60 seconds, filters 75 tons
Pure mellow wine enters above-mentioned target bright beer tank；Turned over from bottom with carbon dioxide and blown 4 minutes, it is ensured that be well mixed in bright beer tank；After tested
Protease A enzyme activity is 9.2 units/ml in wine liquid.
3rd, filling pasteurization
Consider that protease A enzyme activity is still greater than 5 units/ml therefore degerming in the filling laggard tunnel pasteurizer of pure mellow wine
Warm bottle, 55.0 DEG C of highest wine temperature.
4th, bubble holds attenuation verses
(i.e. without blending, gained zymotic fluid stoste is directly filling with former technique to take a collection of product for producing as stated above
Pasteurization) under the product that produces, do instrumental method bubble holding property contrast, two batches product comes from same tank zymotic fluid, as a result as following
Shown in table 1.As shown in Table 1, product has positive effect in terms of slowing down bubble and holding decay as obtained in the method for the invention.
Table 1：
| The method of the invention | Former technique | |
| Proteinase A activity (unit/ml) | 9.2 | 19.5 |
| The bubble that dispatches from the factory holds (s) | 210 | 205 |
| After one month (s) | 205 | 193 |
| After two months (s) | 199 | 184 |
| After three months (s) | 195 | 173 |
| After four months (s) | 193 | 165 |
| After six months (s) | 188 | 158 |
| Attenuation rate (%) | 11.6% | 23.0% |
Embodiment 2
Draft beer, 360 days shelf-lifves are produced using the production line of the applicant, fermentation uses B yeast, the cohesion of B yeast
Property good, recovery time morning, need 6~8 days, be adapted to 10~12 DEG C of higher temperature fermentation, protease A dissolution is less.Production decision
It is as follows：
1st, ratio-dependent is blent：
Routinely technique obtains maturing fermentation liquid, collects 20 tank zymotic fluid data, including：
1) protease A Enzyme activity assay：Pure mellow wine detects protease A enzyme activity using fluorogenic substrate method after filtering, and average enzyme activity shows
Show 15.0 units/ml, fluctuation range is in 13~17 units/ml；
2) ratio primary election is blent：Relatively long for beer product in view of 360 day shelf-life, protease A enzyme is subjected to
Scope is≤5 units/ml, and it is 2 that enzyme wine liquid of going out blends Proportionality design with stoste:1~3:1；
3) invertase enzyme activity verification：Take wine liquid after the normal filtration of part and be warming up to 80 DEG C and be incubated 10 minutes, it is ensured that sugarcane
Sugared invertase complete deactivation, test paper test is negative, and is cooled to 20 DEG C of normal temperature, and 2 are pressed respectively with stoste:1、3:1 blends 2 parts of samples
Product, carry out sucrose inversion enzyme test peper test again, and test result is shown as strong positive, weakly positive；
Determine to blend ratio afterwards：Choose test result display strong positive and the maximum ratio of enzyme wine liquid accounting of going out, i.e., it is right
The Fruit variety 2:1 is most preferably to blend ratio；
2nd, pure mellow wine blends production, as a example by producing 100 tons of pure mellow wines：
Maturing fermentation liquid is filtered by existing routine operation, 4 tons of pure mellow wines of filter 23 enter target bright beer tank；Afterwards in warp
Instantaneous sterilization thin plate is accessed after conventional filtration flow, sterilization temperature is set and is set 74 DEG C, sterilizing time is set 60 seconds, filters 66 tons
Pure mellow wine enters above-mentioned target bright beer tank；Turned over from bottom with carbon dioxide and blown 4 minutes, it is ensured that be well mixed in bright beer tank；After tested
Protease A enzyme activity is 4.0 units/ml in wine liquid.
3rd, filling sterilizing
Consider protease A enzyme activity it is equally not high already less than 5 units/ml, i.e. sucrase activity, this, it is filling before make
It is degerming with 0.6 micron and 0.45 micron of double-filtration film low temperature.
4th, bubble holds attenuation verses
(i.e. without blending, gained zymotic fluid stoste directly uses film with former technique to take a collection of product for producing as stated above
Carry out filtration sterilization) under the product that produces, do instrumental method bubble holding property contrast, two batches product comes from same tank zymotic fluid, as a result such as
Shown in table 2 below.As shown in Table 2, product has positive effect in terms of slowing down bubble and holding decay as obtained in the method for the invention.
Table 2：
Claims (5)
1. in beer production proteinase A activity control method, it is characterised in that：Obtain maturing fermentation liquid and carry out routine
Filter operation, obtains zymotic fluid stoste；Partial fermentation liquid stoste is carried out into high-temperature instantaneous sterilization afterwards, wine liquid after the enzyme that obtains going out；
Wine liquid and zymotic fluid stoste after the enzyme that goes out finally is taken to be blent, in control gained wine liquid sucrose inversion enzyme test peper positive test and
Protease A enzyme activity≤10 unit/ml in wine liquid, is carried out filling after the completion of blending.
2. control method according to claim 1, it is characterised in that：When blending, sucrose inversion in control gained wine liquid
Protease A enzyme activity is 5~10 units/ml in enzyme test peper positive test and wine liquid.
3. control method according to claim 1 and 2, it is characterised in that：Once removed again before filling the container or after filling
Bacterium is processed.
4. control method according to claim 3, it is characterised in that：Sucrose inversion enzyme test peper is surveyed in gained wine liquid is blent
Examination is positive and in wine liquid during protease A enzyme activity >=5 unit/ml, and the pasteurization that PU values are 2~3 is used after filling.
5. control method according to claim 3, it is characterised in that：Sucrose inversion enzyme test peper is surveyed in gained wine liquid is blent
Examination is positive and protease A enzyme activity≤5 unit/ml in wine liquid, degerming using micro-filtrate membrane filtration before filling the container.
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| Application Number | Priority Date | Filing Date | Title |
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| CN201710195337.6A CN106867731A (en) | 2017-03-28 | 2017-03-28 | The control method of proteinase A activity in beer production |
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| Application Number | Priority Date | Filing Date | Title |
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| CN201710195337.6A CN106867731A (en) | 2017-03-28 | 2017-03-28 | The control method of proteinase A activity in beer production |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111398537A (en) * | 2020-04-25 | 2020-07-10 | 燕京啤酒(曲阜三孔)有限责任公司 | Method for predicting and regulating bubble-holding index of finished beer |
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|---|---|---|---|---|
| CN1546525A (en) * | 2003-12-08 | 2004-11-17 | 江南大学 | A kind of extraction method and application of protease A inhibitor |
| CN1995324A (en) * | 2006-12-27 | 2007-07-11 | 江南大学 | Prolease A defective yeast suitable for pure draft beer brewage and its usage method |
| CN103387898A (en) * | 2013-07-15 | 2013-11-13 | 燕京啤酒(桂林漓泉)股份有限公司 | 7 DEG P low-alcohol beer and preparation method thereof |
| CN103589549A (en) * | 2013-10-16 | 2014-02-19 | 江苏大富豪酿酒科技发展有限公司 | A kind of production method of pure draft beer |
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2017
- 2017-03-28 CN CN201710195337.6A patent/CN106867731A/en active Pending
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1546525A (en) * | 2003-12-08 | 2004-11-17 | 江南大学 | A kind of extraction method and application of protease A inhibitor |
| CN1995324A (en) * | 2006-12-27 | 2007-07-11 | 江南大学 | Prolease A defective yeast suitable for pure draft beer brewage and its usage method |
| CN103387898A (en) * | 2013-07-15 | 2013-11-13 | 燕京啤酒(桂林漓泉)股份有限公司 | 7 DEG P low-alcohol beer and preparation method thereof |
| CN103589549A (en) * | 2013-10-16 | 2014-02-19 | 江苏大富豪酿酒科技发展有限公司 | A kind of production method of pure draft beer |
Non-Patent Citations (1)
| Title |
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| 陈旭等: "蛋白酶A与纯生啤酒泡沫稳定性及蔗糖转化酶的关系研究", 《酿酒科技》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111398537A (en) * | 2020-04-25 | 2020-07-10 | 燕京啤酒(曲阜三孔)有限责任公司 | Method for predicting and regulating bubble-holding index of finished beer |
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Application publication date: 20170620 |