2.43
1.65
1.98
0.73
1.88
1.81
2.43
2.2 Sylweddau safonol a ddefnyddir yng nghromlin calibradu dosbarthiad màs moleciwlaidd cymharol: inswlin, mycopeptidau, glysin-glycin-tyrosin-arginin, glysin-glycin-glycin
3 Offeryn ac offer
23.2
21.4
22.2
16.1
22.3
20.8
23.9
27.5
At ei gilydd, mae cyfran yr asidau amino yng nghynhyrchion Sustar yn uwch na'r gyfran yng nghynhyrchion Zinpro.
Rhan 8 Effeithiau defnydd
Effaith gwahanol ffynonellau o fwynau hybrin ar berfformiad cynhyrchu ac ansawdd wyau ieir dodwy yn y cyfnod dodwy hwyr
Proses Gynhyrchu
Technoleg chelation wedi'i thargedu
Technoleg emwlsio cneifio
Technoleg chwistrellu pwysau a sychu
Technoleg oeri a dadleithio
Technoleg rheoli amgylcheddol uwch
Atodiad A: Dulliau ar gyfer Pennu dosbarthiad màs moleciwlaidd cymharol peptidau
Mabwysiadu safon: GB/T 22492-2008
1 Egwyddor Prawf:
Fe'i penderfynwyd drwy gromatograffaeth hidlo gel perfformiad uchel. Hynny yw, gan ddefnyddio llenwr mandyllog fel cyfnod llonydd, yn seiliedig ar y gwahaniaeth ym maint màs moleciwlaidd cymharol cydrannau'r sampl ar gyfer gwahanu, a ganfuwyd ar y bond peptid o donfedd amsugno uwchfioled o 220nm, gan ddefnyddio'r feddalwedd prosesu data bwrpasol ar gyfer pennu dosbarthiad màs moleciwlaidd cymharol drwy gromatograffaeth hidlo gel (h.y., y feddalwedd GPC), proseswyd y cromatogramau a'u data, a'u cyfrifwyd i gael maint màs moleciwlaidd cymharol y peptid ffa soia a'r ystod ddosbarthu.
2. Adweithyddion
Dylai'r dŵr arbrofol fodloni manyleb dŵr eilaidd yn GB/T6682, mae'r defnydd o adweithyddion, ac eithrio darpariaethau arbennig, yn bur yn ddadansoddol.
2.1 Mae adweithyddion yn cynnwys asetonitril (pur yn gromatograffig), asid trifflworasetig (pur yn gromatograffig),
2.2 Sylweddau safonol a ddefnyddir yng nghromlin calibradu dosbarthiad màs moleciwlaidd cymharol: inswlin, mycopeptidau, glysin-glycin-tyrosin-arginin, glysin-glycin-glycin
3 Offeryn ac offer
3.1 Cromatograff Hylif Perfformiad Uchel (HPLC): gweithfan neu integreiddiwr cromatograffig gyda synhwyrydd UV a meddalwedd prosesu data GPC.
3.2 Uned hidlo gwactod a dadnwyo cyfnod symudol.
3.3 Balans electronig: gwerth graddol 0.000 1g.
4 Cam gweithredu
4.1 Amodau cromatograffig ac arbrofion addasu system (amodau cyfeirio)
- 4.1.1 Colofn cromatograffig: TSKgelG2000swxl300 mm × 7.8 mm (diamedr mewnol) neu golofnau gel eraill o'r un math â pherfformiad tebyg sy'n addas ar gyfer pennu proteinau a peptidau.
- 4.1.2 Cyfnod symudol: Asetonitril + dŵr + asid trifflworasetig = 20 + 80 + 0.1.
- 4.1.3 Tonfedd canfod: 220 nm.
- 4.1.4 Cyfradd llif: 0.5 mL/mun.
- 4.1.5 Amser canfod: 30 munud.
- 4.1.6 Cyfaint chwistrelliad sampl: 20μL.
- 4.1.7 Tymheredd y golofn: tymheredd yr ystafell.
- 4.1.8 Er mwyn sicrhau bod y system gromatograffig yn bodloni'r gofynion canfod, nodwyd, o dan yr amodau cromatograffig uchod, nad oedd effeithlonrwydd colofn cromatograffig y gel, h.y., nifer damcaniaethol y platiau (N), yn llai na 10000 wedi'i gyfrifo ar sail copaon y safon tripeptid (Glycine-Glycine-Glycine).
- 4.2 Cynhyrchu cromliniau safonol màs moleciwlaidd cymharol
- Paratowyd y gwahanol atebion safonol peptid màs moleciwlaidd cymharol uchod gyda chrynodiad màs o 1 mg / mL trwy baru cyfnod symudol, eu cymysgu mewn cyfran benodol, ac yna eu hidlo trwy bilen cyfnod organig gyda maint mandwll o 0.2 μm ~ 0.5 μm a'u chwistrellu i'r sampl, ac yna cafwyd cromatogramau'r safonau. Cafwyd cromliniau calibradu màs moleciwlaidd cymharol a'u hafaliadau trwy blotio logarithm y màs moleciwlaidd cymharol yn erbyn amser cadw neu drwy atchweliad llinol.
4.3 Triniaeth sampl
Pwyswch 10mg o sampl yn gywir mewn fflasg folwmetrig 10mL, ychwanegwch ychydig o gam symudol, ysgwydwch ag uwchsonig am 10 munud, fel bod y sampl wedi'i doddi'n llwyr a'i gymysgu, ei wanhau â'r cam symudol i'r raddfa, ac yna ei hidlo trwy bilen cam organig gyda maint mandwll o 0.2μm ~ 0.5μm, a dadansoddwyd y hidlif yn ôl yr amodau cromatograffig yn A.4.1.
- 5. Cyfrifo dosbarthiad màs moleciwlaidd cymharol
- Ar ôl dadansoddi'r toddiant sampl a baratowyd yn 4.3 o dan amodau cromatograffig 4.1, gellir cael màs moleciwlaidd cymharol y sampl a'i ystod ddosbarthu trwy amnewid data cromatograffig y sampl yn y gromlin calibradu 4.2 gyda meddalwedd prosesu data GPC. Gellir cyfrifo dosbarthiad màsau moleciwlaidd cymharol y gwahanol peptidau trwy'r dull normaleiddio arwynebedd brig, yn ôl y fformiwla: X=A/A cyfanswm×100
- Yn y fformiwla: X - Cyfran màs peptid màs moleciwlaidd cymharol yn y peptid cyfan yn y sampl, %;
- A - Arwynebedd brig peptid màs moleciwlaidd cymharol;
- Cyfanswm A - swm arwynebeddau brig pob peptid màs moleciwlaidd cymharol, wedi'i gyfrifo i un lle degol.
- 6 Ailadroddadwyedd
- Ni ddylai'r gwahaniaeth absoliwt rhwng dau benderfyniad annibynnol a gafwyd o dan amodau ailadroddadwyedd fod yn fwy na 15% o gymedr rhifyddol y ddau benderfyniad.
- Atodiad B: Dulliau ar gyfer Pennu Asidau Amino Rhydd
- Mabwysiadu safon: Q/320205 KAVN05-2016
- 1.2 Adweithyddion a deunyddiau
- Asid asetig rhewlifol: pur yn ddadansoddol
- Asid perclorig: 0.0500 mol/L
- Dangosydd: dangosydd fioled grisial 0.1% (asid asetig rhewlifol)
- 2. Penderfynu ar asidau amino rhydd
Sychwyd y samplau ar 80°C am 1 awr.
Rhowch y sampl mewn cynhwysydd sych i oeri'n naturiol i dymheredd ystafell neu i oeri i dymheredd defnyddiadwy.Pwyswch tua 0.1 g o sampl (cywir i 0.001 g) i mewn i fflasg gonigol sych 250 mL.Ewch ymlaen yn gyflym i'r cam nesaf i osgoi'r sampl rhag amsugno lleithder amgylchynolYchwanegwch 25 mL o asid asetig rhewlifol a chymysgwch yn dda am ddim mwy na 5 munud.Ychwanegwch 2 ddiferyn o ddangosydd fioled grisialTitradu gyda 0.0500 mol / L (±0.001) o doddiant titradu safonol o asid perclorig nes bod y toddiant yn newid o borffor i'r pwynt terfynol.
Cofnodwch gyfaint y toddiant safonol a ddefnyddiwyd.
- Gwnewch y prawf gwag ar yr un pryd.
- 3. Cyfrifiad a chanlyniadau
- Mynegir cynnwys yr asid amino rhydd X yn yr adweithydd fel ffracsiwn màs (%) a chaiff ei gyfrifo yn ôl y fformiwla: X = C × (V1-V0) × 0.1445/M × 100%, yn y fformiwla:
- C - Crynodiad hydoddiant asid perclorig safonol mewn molau fesul litr (mol/L)
- V1 - Cyfaint a ddefnyddir ar gyfer titradu samplau gyda hydoddiant asid perclorig safonol, mewn mililitrau (mL).
- Vo - Cyfaint a ddefnyddir ar gyfer titradiad blank gyda hydoddiant asid perclorig safonol, mewn mililitrau (mL);
M - Màs y sampl, mewn gramau (g).
| 0.1445: Màs cyfartalog asidau amino sy'n cyfateb i 1.00 mL o doddiant asid perclorig safonol [c (HClO4) = 1.000 mol / L]. | 4.2.3 Toddiant titradiad safonol ceriwm sylffad: crynodiad c [Ce (SO4) 2] = 0.1 mol/L, wedi'i baratoi yn ôl GB/T601. | |
| Mabwysiadu safonau: Q/70920556 71-2024 | 1. Egwyddor pennu (Fe fel enghraifft) | Mae gan gymhlygion haearn asid amino hydoddedd isel iawn mewn ethanol anhydrus ac mae ïonau metel rhydd yn hydoddadwy mewn ethanol anhydrus, defnyddiwyd y gwahaniaeth mewn hydoddedd rhwng y ddau mewn ethanol anhydrus i bennu cyfradd chelation cymhlygion haearn asid amino. |
| Yn y fformiwla: V1 - cyfaint y toddiant safonol sylffad ceriwm a ddefnyddir ar gyfer titradu'r toddiant prawf, mL; | Ethanol anhydrus; mae'r gweddill yr un fath â chymal 4.5.2 yn GB/T 27983-2011. | 3. Camau dadansoddi |
| Gwnewch ddau brawf ochr yn ochr. Pwyswch 0.1g o'r sampl wedi'i sychu ar 103±2℃ am 1 awr, yn gywir i 0.0001g, ychwanegwch 100mL o ethanol anhydrus i'w doddi, hidlwch, hidlwch y gweddillion a olchwch â 100mL o ethanol anhydrus am o leiaf dair gwaith, yna trosglwyddwch y gweddillion i fflasg gonigol 250mL, ychwanegwch 10mL o doddiant asid sylffwrig yn unol â chymal 4.5.3 yn GB/T27983-2011, ac yna cyflawnwch y camau canlynol yn unol â chymal 4.5.3 “Gwreswch i doddi ac yna gadewch i oeri” yn GB/T27983-2011. Cynhaliwch y prawf gwag ar yr un pryd. | 4. Pennu cyfanswm cynnwys haearn | 4.1 Mae'r egwyddor benderfynu yr un fath â chymal 4.4.1 yn GB/T 21996-2008. |
4.2. Adweithyddion a Thoddiannau
| 4.2.1 Asid cymysg: Ychwanegwch 150mL o asid sylffwrig a 150mL o asid ffosfforig at 700mL o ddŵr a chymysgwch yn dda. | 4.2.2 Toddiant dangosydd sodiwm diphenylamin sylffonad: 5g/L, wedi'i baratoi yn ôl GB/T603. | 4.2.3 Toddiant titradiad safonol ceriwm sylffad: crynodiad c [Ce (SO4) 2] = 0.1 mol/L, wedi'i baratoi yn ôl GB/T601. | |
| 4.3 Camau dadansoddi | Gwnewch ddau brawf ochr yn ochr. Pwyswch 0.1g o sampl, yn gywir i 020001g, rhowch mewn fflasg gonigol 250mL, ychwanegwch 10mL o asid cymysg, ar ôl diddymu, ychwanegwch 30ml o ddŵr a 4 diferyn o doddiant dangosydd sodiwm dianilin sylffonad, ac yna cyflawnwch y camau canlynol yn unol â chymal 4.4.2 yn GB/T21996-2008. Cynhaliwch y prawf gwag ar yr un pryd. | 4.4 Cynrychiolaeth o ganlyniadau | Cyfrifwyd cyfanswm cynnwys haearn X1 y cyfadeiladau haearn asid amino o ran cyfran màs haearn, y gwerth a fynegir mewn %, yn ôl fformiwla (1): |
| X1=(V-V0)×C×M×10-3×100 | V0 - toddiant safonol ceriwm sylffad a ddefnyddiwyd ar gyfer titradu toddiant gwag, mL; | V0 - toddiant safonol ceriwm sylffad a ddefnyddiwyd ar gyfer titradu toddiant gwag, mL; | C - Crynodiad gwirioneddol hydoddiant safonol ceriwm sylffad, mol/L5. Cyfrifo cynnwys haearn mewn cheladauCyfrifwyd cynnwys haearn X2 yn y chelad o ran cyfran màs yr haearn, y gwerth a fynegir mewn %, yn ôl y fformiwla: x2 = ((V1-V2) × C × 0.05585)/m1 × 100 |
| Yn y fformiwla: V1 - cyfaint y toddiant safonol sylffad ceriwm a ddefnyddir ar gyfer titradu'r toddiant prawf, mL; | V2 - toddiant safonol ceriwm sylffad a ddefnyddiwyd ar gyfer titradu toddiant gwag, mL;nom1-Màs y sampl, g. Cymerwch gymedr rhifyddol y canlyniadau penderfyniad cyfochrog fel y canlyniadau penderfyniad, ac nid yw'r gwahaniaeth absoliwt rhwng canlyniadau'r penderfyniad cyfochrog yn fwy na 0.3%. | 0.05585 - màs haearn fferrus wedi'i fynegi mewn gramau sy'n cyfateb i 1.00 mL o doddiant safonol ceriwm sylffad C[Ce(SO4)2.4H20] = 1.000 mol/L.nom1-Màs y sampl, g. Cymerwch gymedr rhifyddol y canlyniadau penderfyniad cyfochrog fel y canlyniadau penderfyniad, ac nid yw'r gwahaniaeth absoliwt rhwng canlyniadau'r penderfyniad cyfochrog yn fwy na 0.3%. | 6. Cyfrifo cyfradd chelationCyfradd chelation X3, y gwerth wedi'i fynegi mewn %, X3 = X2/X1 × 100Atodiad C: Dulliau ar gyfer Pennu cyfradd chelation Zinpro |
Mabwysiadu safon: Q/320205 KAVNO7-2016
1. Adweithyddion a deunyddiau
a) Asid asetig rhewlifol: pur yn ddadansoddol; b) Asid perclorig: 0.0500mol/L; c) Dangosydd: dangosydd fioled grisial 0.1% (asid asetig rhewlifol)
2. Penderfynu ar asidau amino rhydd
2.1 Sychwyd y samplau ar 80°C am 1 awr.
2.2 Rhowch y sampl mewn cynhwysydd sych i oeri'n naturiol i dymheredd ystafell neu i oeri i dymheredd defnyddiadwy.
2.3 Pwyswch tua 0.1 g o sampl (cywir i 0.001 g) i mewn i fflasg gonigol sych 250 mL
2.4 Ewch ymlaen yn gyflym i'r cam nesaf i atal y sampl rhag amsugno lleithder amgylchynol.
2.5 Ychwanegwch 25mL o asid asetig rhewlifol a chymysgwch yn dda am ddim mwy na 5 munud.
2.6 Ychwanegwch 2 ddiferyn o ddangosydd fioled grisial.
2.7 Titradu gyda thoddiant titradu safonol 0.0500mol/L (±0.001) o asid perclorig nes bod yr hydoddiant yn newid o borffor i wyrdd am 15 eiliad heb newid lliw fel y pwynt terfyn.
2.8 Cofnodwch gyfaint y toddiant safonol a ddefnyddiwyd.
2.9 Cynhaliwch y prawf gwag ar yr un pryd.
- 3. Cyfrifiad a chanlyniadau
- Catalaneg
- Physicochemical parameters
V1 - Cyfaint a ddefnyddir ar gyfer titradu samplau gyda hydoddiant asid perclorig safonol, mewn mililitrau (mL).
Vo - Cyfaint a ddefnyddir ar gyfer titradiad blank gyda hydoddiant asid perclorig safonol, mewn mililitrau (mL);
c) Chelation rate: ≥ 95%
d) Arsenic: ≤ 2 mg/kg
e) Lead: ≤ 5 mg/kg
f) Cadmium: ≤ 5 mg/kg
g) Moisture content: ≤ 5.0%
h) Fineness: All particles pass through 20 mesh, with a main particle size of 60-80 mesh
Cyfeiriad: Rhif 147 Heol Qingpu, Tref Shouan, Sir Pujiang, Dinas Chengdu, Talaith Sichuan, Tsieina
Ffôn: 86-18880477902
Cynhyrchion
Mwynau olrhain anorganig
- Mwynau olrhain organig
- Swahili
- Gwasanaeth wedi'i addasu
- Dolenni cyflym
Proffil y Cwmni
| Application object | Suggested dosage (g/t full-value material) | Content in full-value feed (mg/kg) | Efficacy |
| Gwjarataidd | Cliciwch am ymholiad | © Hawlfraint - 2010-2025: Cedwir Pob Hawl. | Map o'r Wefan CHWILIAD UCHAF Ffôn |
| Ffôn | 86-18880477902 | Javaneg | E-bost |
| 8618880477902 | Tsieineaidd | Ffrangeg | |
| Bird | Tsieineaidd | Ffrangeg | Almaeneg Sbaeneg |
| Aquatic animals | Japaneg | Coreeg | Arabeg Groeg |
| Twrceg | Eidaleg | ||
| Ruminant animal g/head day | January 0.75 | Indoneseg Affricaneg Swedeg |
Pwyleg
- Basgeg
- Catalaneg
- Physicochemical parameters
Hindi
Laoaidd
c) Chelation rate: ≥ 95%
d) Arsenic: ≤ 2 mg/kg
e) Lead: ≤ 5 mg/kg
f) Cadmium: ≤ 5 mg/kg
g) Moisture content: ≤ 5.0%
h) Fineness: All particles pass through 20 mesh, with a main particle size of 60-80 mesh
Shona
Bwlgareg
- Cebuano
- This product is chemically stable and can significantly reduce its damage to vitamins and fats, etc. The use of this product is conducive to improving feed quality;
- The product is absorbed through small peptide and amino acid pathways, reducing the competition and antagonism with other trace elements, and has the best bio-absorption and utilization rate;
- Croateg
Iseldireg
| Application object | Wrdw Fietnameg | Content in full-value feed (mg/kg) | Efficacy |
| Gwjarataidd | Haitian | Hausa | Kinyarwanda Hmong Hwngareg |
| Piglets and fattening pigs | Igbo | Javaneg | Kannada Khmer Cwrdeg |
| Cirgiseg | Lladin | ||
| Bird | 300～400 | 45～60 | Macedoneg Malayeg Malayalam |
| Aquatic animals | 200～300 | 30～45 | 1. Promote growth, improve feed conversion; 2. Improve anti-stress abolity, reduce morbidity and mortality. |
Norwyeg
- Pashto
- Appearance: brownish-yellow granules
- Physicochemical parameters
Serbaidd
Sesotho
c) Chelation rate: ≥ 95%
d) Arsenic: ≤ 2 mg/kg
e) Lead: ≤ 5 mg/kg
f) Cadmium: ≤ 5 mg/kg
g) Moisture content: ≤ 5.0%
h) Fineness: All particles pass through 20 mesh, with a main particle size of 60-80 mesh
Shona
Sindhi
This product is an all-organic trace mineral chelated by a special chelating proces with pure plant enzymatic small molecule peptides as chelating substrates and trace elements;
Swahili
Tajic
Tamil
Telugu
Thai
| Application object | Wrdw Fietnameg | Content in full-value feed (mg/kg) | Efficacy |
| Iddew-Almaeneg | Yoruba | Swlw | Kinyarwanda Oriya Tyrcmeneg |
| Uyghur | 250～400 | 37.5～60 | 1. Improving the immunity of piglets, reducing diarrhea and mortality; 2. Improving palatability, increasing feed intake, increasing growth rate and improving feed conversion; 3. Make the pig coat bright and improve the carcass quality and meat quality. |
| Bird | 300～400 | 45～60 | 1. Improve feather glossiness; 2. improve the laying rate, fertilization rate and hatching rate of breeding eggs, and strengthen the coloring ability of egg yolk; 3. Improve anti-stress ability and reduce mortality; 4. Improve feed conversion and increase growth rate. |
| Aquatic animals | January 300 | 45 | 1. Promote growth, improve feed conversion; 2. Improve anti-stress abolity, reduce morbidity and mortality. |
| Ruminant animal g/head day | 2.4 | 1. Improve milk yield, prevent mastitis and foof rot, and reduce somatic cell content in milk; 2. Promote growth, improve feed conversion and improve meat quality. |
4. Manganese Amino Acid Chelate Feed Grade
- Product Name: Manganese Amino Acid Chelate Feed Grade
- Appearance: brownish-yellow granules
- Physicochemical parameters
a) Mn: ≥ 10.0%
b) Total amino acids: ≥ 19.5%
c) Chelation rate: ≥ 95%
d) Arsenic: ≤ 2 mg/kg
e) Lead: ≤ 5 mg/kg
f) Cadmium: ≤ 5 mg/kg
g) Moisture content: ≤ 5.0%
h) Fineness: All particles pass through 20 mesh, with a main particle size of 60-80 mesh
n=0, 1,2,...indicates chelated manganese for dipeptides, tripeptides, and tetrapeptides
Characteristics of Manganese Amino Acid Chelate Feed Grade
This product is an all-organic trace mineral chelated by a special chelating proces with pure plant enzymatic small molecule peptides as chelating substrates and trace elements;
This product is chemically stable and can significantly reduce its damage to vitamins and fats, etc. The use of this product is conducive to improving feed quality;
The product is absorbed through small peptide and amino acid pathways, reducing the competition and antagonism with other trace elements, and has the best bio-absorption and utilization rate;
The product can improve the growth rate, improve feed conversion and health status significantly; and improve the laying rate, hatching rate and healthy chick rate of breeding poultry obviously;
Manganese is necessary for bone growth and connective tissue maintenance. It is closely related to many enzymes; and participates in carbohydrate, fat and protein metabolism, reproduction and immune response.
Usage and Efficacy of Manganese Amino Acid Chelate Feed Grade
| Application object | Suggested dosage (g/t full-value material) | Content in full-value feed (mg/kg) | Efficacy |
| Breeding pig | 200～300 | 30～45 | 1. Promote the normal development of sexual organs and improve sperm motility; 2. Improve the reproductive capacity of breeding pigs and reduce reproductive obstacles. |
| Piglets and fattening pigs | 100～250 | 15～37.5 | 1. It is beneficial to improve immune functions, and improve anti-stress ability and disease resistance; 2. Promote growth and improve feed conversion significantly; 3. Improve meat color and quality, and improve lean meat percentage. |
| Bird | 250～350 | 37.5～52.5 | 1. Improve anti-stress ability and reduce mortality; 2. Improve laying rate, fertilization rate and hatching rate of breeding eggs, improve eggshell quality and reduce shell breaking rate; 3. Promote bone growth and reduce the incidence of leg diseases. |
| Aquatic animals | 100～200 | 15～30 | 1. Promote growth and improve its anti-stress ability and disease resistance; 2. Improve sperm motility and hatching rate of fertilized eggs. |
| Ruminant animal g/head day | Cattle 1.25 | 1. Prevent fatty acid synthesis disorder and bone tissue damage; 2. Improve reproductive capacity, prevent abortion and postpartum paralysis of female animals, reduce the mortality of calves and lambs, and increase the newborn weight of young animals. | |
| Goat 0.25 |
Part 6 FAB of Small Peptide-mineral Chelates
| S/N | F: Functional attributes | A: Competitive differences | B: Benefits brought by competitive differences to users |
| 1.52 | Selectivity control of raw materials | Select pure plant enzymatic hydrolysis of small peptides | High biological safety, avoiding cannibalism |
| 2 | Directional digestion technology for double protein biological enzyme | High proportion of small molecular peptides | More "targets", which are not easy to saturation, with high biological activity and better stability |
| 3 | Advanced pressure spray & drying technology | Granular product, with uniform particle size, better fluidity, not easy to absorb moisture | Ensure easy to use, more uniform mixing in complete feed |
| Low water content (≤ 5%), which greatly reduces the influence caused by vitamins and enzyme preparations | Improve the stability of feed products | ||
| 4 | Advanced production control technology | Totally enclosed process, high degree of automatic control | Safe and stable quality |
| 5 | Advanced quality control technology | Establish and improve scientific and advanced analytical methods and control means for detecting factors affecting product quality, such as acid-soluble protein, molecular weight distribution, amino acids and chelating rate | Ensure quality, ensure efficiency and improve efficiency |
Part 7 Competitor Comparison
Standard VS Standard
Comparison of peptide distribution and chelation rate of products
| Sustar's products | Proportion of small peptides（180-500） | Zinpro's products | Proportion of small peptides（180-500） |
| AA-Cu | ≥74% | AVAILA-Cu | 78% |
| AA-Fe | ≥48% | AVAILA-Fe | 59% |
| AA-Mn | ≥33% | AVAILA-Mn | 53% |
| AA-Zn | ≥37% | AVAILA-Zn | 56% |
| Sustar's products | Chelation rate | Zinpro's products | Chelation rate |
| AA-Cu | 94.8% | AVAILA-Cu | 94.8% |
| AA-Fe | 95.3% | AVAILA-Fe | 93.5% |
| AA-Mn | 94.6% | AVAILA-Mn | 94.6% |
| AA-Zn | 97.7% | AVAILA-Zn | 90.6% |
The ratio of small peptides of Sustar is slightly lower than that of Zinpro, and the chelation rate of Sustar's products is slightly higher than that of Zinpro's products.
Comparison of the content of 17 amino acids in different products
| Name of amino acids | Sustar's Copper Amino Acid Chelate Feed Grade | Zinpro's AVAILA copper | Sustar's Ferrous Amino Acid C helate Feed Grade | Zinpro's AVAILA iron | Sustar's Manganese Amino Acid Chelate Feed Grade | Zinpro's AVAILA manganese | Sustar's Zinc Amino Acid Chelate Feed Grade | Zinpro's AVAILA zinc |
| aspartic acid (%) | 1.88 | 0.72 | 1.50 | 0.56 | 1.78 | 1.47 | 1.80 | 2.09 |
| glutamic acid (%) | 4.08 | 6.03 | 4.23 | 5.52 | 4.22 | 5.01 | 4.35 | 3.19 |
| Serine (%) | 0.86 | 0.41 | 1.08 | 0.19 | 1.05 | 0.91 | 1.03 | 2.81 |
| Histidine (%) | 0.56 | 0.00 | 0.68 | 0.13 | 0.64 | 0.42 | 0.61 | 0.00 |
| Glycine (%) | 1.96 | 4.07 | 1.34 | 2.49 | 1.21 | 0.55 | 1.32 | 2.69 |
| Threonine (%) | 0.81 | 0.00 | 1.16 | 0.00 | 0.88 | 0.59 | 1.24 | 1.11 |
| Arginine (%) | 1.05 | 0.78 | 1.05 | 0.29 | 1.43 | 0.54 | 1.20 | 1.89 |
| Alanine (%) | 2.85 | 1.52 | 2.33 | 0.93 | 2.40 | 1.74 | 2.42 | 1.68 |
| Tyrosinase (%) | 0.45 | 0.29 | 0.47 | 0.28 | 0.58 | 0.65 | 0.60 | 0.66 |
| Cystinol (%) | 0.00 | 0.00 | 0.09 | 0.00 | 0.11 | 0.00 | 0.09 | 0.00 |
| Valine (%) | 1.45 | 1.14 | 1.31 | 0.42 | 1.20 | 1.03 | 1.32 | 2.62 |
| Methionine (%) | 0.35 | 0.27 | 0.72 | 0.65 | 0.67 | 0.43 | January 0.75 | 0.44 |
| Phenylalanine (%) | 0.79 | 0.41 | 0.82 | 0.56 | 0.70 | 1.22 | 0.86 | 1.37 |
| Isoleucine (%) | 0.87 | 0.55 | 0.83 | 0.33 | 0.86 | 0.83 | 0.87 | 1.32 |
| Leucine (%) | 2.16 | 0.90 | 2.00 | 1.43 | 1.84 | 3.29 | 2.19 | 2.20 |
| Lysine (%) | 0.67 | 2.67 | 0.62 | 1.65 | 0.81 | 0.29 | 0.79 | 0.62 |
| Proline (%) | 2.43 | 1.65 | 1.98 | 0.73 | 1.88 | 1.81 | 2.43 | 2.78 |
| Total amino acids (%) | 23.2 | 21.4 | 22.2 | 16.1 | 22.3 | 20.8 | 23.9 | 27.5 |
Overall, the proportion of amino acids in Sustar's products is higher than that in Zinpro's products.
Part 8 Effects of use
Effects of different sources of trace minerals on the production performance and egg quality of laying hens in the late laying period
Production Process
- Targeted chelation technology
- Shear emulsification technology
- Pressure spray & drying technology
- Refrigeration & dehumidification technology
- Advanced environmental control technology
Appendix A: Methods for the Determination of relative molecular mass distribution of peptides
Adoption of standard: GB/T 22492-2008
1 Test Principle:
It was determined by high performance gel filtration chromatography. That is to say, using porous filler as stationary phase, based on the difference in the relative molecular mass size of the sample components for separation, detected at the peptide bond of the ultraviolet absorption wavelength of 220nm, using the dedicated data processing software for the determination of relative molecular mass distribution by gel filtration chromatography (i.e., the GPC software), the chromatograms and their data were processed, calculated to get the size of the relative molecular mass of the soybean peptide and the distribution range.
2. Reagents
The experimental water should meet the specification of secondary water in GB/T6682, the use of reagents, except for special provisions, are analytically pure.
2.1 Reagents include acetonitrile (chromatographically pure), trifluoroacetic acid (chromatographically pure),
2.2 Standard substances used in the calibration curve of relative molecular mass distribution: insulin, mycopeptides, glycine-glycine-tyrosine-arginine, glycine-glycine-glycine
3 Instrument and equipment
3.1 High Performance Liquid Chromatograph (HPLC): a chromatographic workstation or integrator with a UV detector and GPC data processing software.
3.2 Mobile phase vacuum filtration and degassing unit.
3.3 Electronic balance: graduated value 0.000 1g.
4 Operating steps
4.1 Chromatographic conditions and system adaptation experiments (reference conditions)
4.1.1 Chromatographic column: TSKgelG2000swxl300 mm×7.8 mm (inner diameter) or other gel columns of the same type with similar performance suitable for the determination of proteins and peptides.
4.1.2 Mobile phase: Acetonitrile + water + trifluoroacetic acid = 20 + 80 + 0.1.
4.1.3 Detection wavelength: 220 nm.
4.1.4 Flow rate: 0.5 mL/min.
4.1.5 Detection time: 30 min.
4.1.6 Sample injection volume: 20μL.
4.1.7 Column temperature: room temperature.
4.1.8 In order to make the chromatographic system meet the detection requirements, it was stipulated that under the above chromatographic conditions, the gel chromatographic column efficiency, i.e., the theoretical number of plates (N), was not less than 10000 calculated on the basis of the peaks of the tripeptide standard (Glycine-Glycine-Glycine).
4.2 Production of relative molecular mass standard curves
The above different relative molecular mass peptide standard solutions with a mass concentration of 1 mg / mL were prepared by mobile phase matching, mixed in a certain proportion, and then filtered through an organic phase membrane with the pore size of 0.2 μm~0.5 μm and injected into the sample, and then the chromatograms of the standards were obtained. Relative molecular mass calibration curves and their equations were obtained by plotting the logarithm of relative molecular mass against retention time or by linear regression.
4.3 Sample treatment
Accurately weigh 10mg of sample in a 10mL volumetric flask, add a little mobile phase, ultrasonic shaking for 10min, so that the sample is fully dissolved and mixed, diluted with mobile phase to the scale, and then filtered through an organic phase membrane with a pore size of 0.2μm~0.5μm, and the filtrate was analyzed according to the chromatographic conditions in A.4.1.
5. Calculation of relative molecular mass distribution
After analyzing the sample solution prepared in 4.3 under the chromatographic conditions of 4.1, the relative molecular mass of the sample and its distribution range can be obtained by substituting the chromatographic data of the sample into the calibration curve 4.2 with GPC data processing software. The distribution of the relative molecular masses of the different peptides can be calculated by the peak area normalization method, according to the formula: X=A/A total×100
In the formula: X - The mass fraction of a relative molecular mass peptide in the total peptide in the sample, %;
A - Peak area of a relative molecular mass peptide;
Total A - the sum of the peak areas of each relative molecular mass peptide, calculated to one decimal place.
6 Repeatability
The absolute difference between two independent determinations obtained under conditions of repeatability shall not exceed 15% of the arithmetic mean of the two determinations.
Appendix B: Methods for the Determination of Free Amino Acids
Adoption of standard: Q/320205 KAVN05-2016
1.2 Reagents and materials
Glacial acetic acid: analytically pure
Perchloric acid: 0.0500 mol/L
Indicator: 0.1% crystal violet indicator (glacial acetic acid)
2. Determination of free amino acids
The samples were dried at 80°C for 1 hour.
Place the sample in a dry container to cool naturally to room temperature or cool down to a usable temperature.
Weigh approximately 0.1 g of sample (accurate to 0.001 g) into a 250 mL dry conical flask.
Quickly proceed to the next step to avoid the sample from absorbing ambient moisture
Add 25 mL of glacial acetic acid and mix well for no more than 5 min.
Add 2 drops of crystal violet indicator
Titrate with 0.0500 mol / L (±0.001) standard titration solution of perchloric acid until the solution changes from purple to the end point.
Record the volume of standard solution consumed.
Carry out the blank test at the same time.
3. Calculation and results
The free amino acid content X in the reagent is expressed as a mass fraction (%) and is calculated according to the formula: X = C × (V1-V0) × 0.1445/M × 100%, in tne formula:
C - Concentration of standard perchloric acid solution in moles per liter (mol/L)
V1 - Volume used for titration of samples with standard perchloric acid solution, in milliliters (mL).
Vo - Volume used for titration blank with standard perchloric acid solution, in milliliters (mL);
M - Mass of the sample, in grams (g ).
0.1445: Average mass of amino acids equivalent to 1.00 mL of standard perchloric acid solution [c (HClO4) = 1.000 mol / L].
Appendix C: Methods for the Determination of Sustar's chelation rate
Adoption of standards: Q/70920556 71-2024
1. Determination principle (Fe as an example)
Amino acid iron complexes have very low solubility in anhydrous ethanol and free metal ions are soluble in anhydrous ethanol, the difference in solubility between the two in anhydrous ethanol was utilized to determine the chelation rate of amino acid iron complexes.
2. Reagents & Solutions
Anhydrous ethanol; the rest is the same as clause 4.5.2 in GB/T 27983-2011.
3. Steps of analysis
Do two trials in parallel. Weigh 0.1g of the sample dried at 103±2℃ for 1 hour, accurate to 0.0001g, add 100mL of anhydrous ethanol to dissolve, filter, filter residue washed with 100mL of anhydrous ethanol for at least three times, then transfer the residue into a 250mL conical flask, add 10mL of sulfuric acid solution according to clause 4.5.3 in GB/T27983-2011, and then perform the following steps according to clause 4.5.3 “Heat to dissolve and then let cool” in GB/T27983-2011. Carry out the blank test at the same time.
4. Determination of total iron content
4.1 The principle of determination is the same as clause 4.4.1 in GB/T 21996-2008.
4.2. Reagents & Solutions
4.2.1 Mixed acid: Add 150mL of sulfuric acid and 150mL of phosphoric acid to 700mL of water and mix well.
4.2.2 Sodium diphenylamine sulfonate indicator solution: 5g/L, prepared according to GB/T603.
4.2.3 Cerium sulfate standard titration solution: concentration c [Ce (SO4) 2] = 0.1 mol/L, prepared according to GB/T601.
4.3 Steps of analysis
Do two trials in parallel. Weigh 0.1g of sample, accurate to 020001g, place in a 250mL conical flask, add 10mL of mixed acid, after dissolution, add 30ml of water and 4 drops of sodium dianiline sulfonate indicator solution, and then perform the following steps according to clause 4.4.2 in GB/T21996-2008. Carry out the blank test at the same time.
4.4 Representation of results
The total iron content X1 of the amino acid iron complexes in terms of mass fraction of iron, the value expressed in %, was calculated according to formula (1):
X1=(V-V0)×C×M×10-3×100
In the formula: V - volume of cerium sulfate standard solution consumed for titration of test solution, mL;
V0 - cerium sulfate standard solution consumed for titration of blank solution, mL;
C - Actual concentration of cerium sulfate standard solution, mol/L
5. Calculation of iron content in chelates
The iron content X2 in the chelate in terms of the mass fraction of iron, the value expressed in %, was calculated according to the formula: x2 = ((V1-V2) × C × 0.05585)/m1 × 100
In the formula: V1 - volume of cerium sulfate standard solution consumed for titration of test solution, mL;
V2 - cerium sulfate standard solution consumed for titration of blank solution, mL;
C - Actual concentration of cerium sulfate standard solution, mol/L;
0.05585 - mass of ferrous iron expressed in grams equivalent to 1.00 mL of cerium sulfate standard solution C[Ce(SO4)2.4H20] = 1.000 mol/L.
m1-Mass of the sample, g. Take the arithmetic mean of the parallel determination results as the determination results, and the absolute difference of the parallel determination results is not more than 0.3%.
6. Calculation of chelation rate
Chelation rate X3, the value expressed in %, X3 = X2/X1 × 100
Appendix C: Methods for the Determination of Zinpro's chelation rate
Adoption of standard: Q/320205 KAVNO7-2016
1. Reagents and materials
a) Glacial acetic acid: analytically pure; b) Perchloric acid: 0.0500mol/L; c) Indicator: 0.1% crystal violet indicator (glacial acetic acid)
2. Determination of free amino acids
2.1 The samples were dried at 80°C for 1 hour.
2.2 Place the sample in a dry container to cool naturally to room temperature or cool down to a usable temperature.
2.3 Weigh approximately 0.1 g of sample (accurate to 0.001 g) into a 250 mL dry conical flask
2.4 Quickly proceed to the next step to avoid the sample from absorbing ambient moisture.
2.5 Add 25mL of glacial acetic acid and mix well for no more than 5min.
2.6 Add 2 drops of crystal violet indicator.
2.7 Titrate with 0.0500mol/L (±0.001) standard titration solution of perchloric acid until the solution changes from purple to green for 15s without changing color as the end point.
2.8 Record the volume of standard solution consumed.
2.9 Carry out the blank test at the same time.
3. Calculation and results
The free amino acid content X in the reagent is expressed as a mass fraction (%), calculated according to formula (1): X=C×(V1-V0) ×0.1445/M×100%...... .......(1)
In the formula: C - concentration of standard perchloric acid solution in moles per liter (mol/L)
V1 - Volume used for titration of samples with standard perchloric acid solution, in milliliters (mL).
Vo - Volume used for titration blank with standard perchloric acid solution, in milliliters (mL);
M - Mass of the sample, in grams (g ).
0.1445 - Average mass of amino acids equivalent to 1.00 mL of standard perchloric acid solution [c (HClO4) = 1.000 mol / L].
4. Calculation of chelation rate
The chelation rate of the sample is expressed as mass fraction (%), calculated according to formula (2): chelation rate = (total amino acid content - free amino acid content)/total amino acid content×100%.
Post time: Sep-17-2025
