2.43
1.65
1.98
0.73
1.88
1.81
2.43
2.2 Bahan piawai yang digunakan dalam lengkung penentukuran taburan jisim molekul relatif: insulin, mikopeptida, glisin-glisin-tirosin-arginin, glisin-glisin-glisin
3 Instrumen dan peralatan
23.2
21.4
22.2
16.1
22.3
20.8
23.9
27.5
Secara keseluruhan, kadar asid amino dalam produk Sustar adalah lebih tinggi daripada produk Zinpro.
Bahagian 8 Kesan penggunaan
Kesan pelbagai sumber mineral surih terhadap prestasi pengeluaran dan kualiti telur ayam petelur pada tempoh bertelur lewat
Proses Pengeluaran
Teknologi khelasi yang disasarkan
Teknologi pengemulsian ricih
Teknologi semburan & pengeringan tekanan
Teknologi penyejukan & penyahlembapan
Teknologi kawalan alam sekitar yang canggih
Lampiran A: Kaedah untuk Penentuan taburan jisim molekul relatif peptida
Penerimaan piawaian: GB/T 22492-2008
1 Prinsip Ujian:
Ia ditentukan melalui kromatografi penapisan gel berprestasi tinggi. Iaitu, menggunakan pengisi berliang sebagai fasa pegun, berdasarkan perbezaan saiz jisim molekul relatif komponen sampel untuk pemisahan, yang dikesan pada ikatan peptida bagi panjang gelombang penyerapan ultraungu 220 nm, menggunakan perisian pemprosesan data khusus untuk penentuan taburan jisim molekul relatif melalui kromatografi penapisan gel (iaitu, perisian GPC), kromatogram dan datanya diproses, dikira untuk mendapatkan saiz jisim molekul relatif peptida kacang soya dan julat taburan.
2. Reagen
Air eksperimen hendaklah memenuhi spesifikasi air sekunder dalam GB/T6682, penggunaan reagen, kecuali untuk peruntukan khas, adalah tulen secara analitikal.
2.1 Reagen termasuk asetonitril (tulen secara kromatografi), asid trifluoroasetik (tulen secara kromatografi),
2.2 Bahan piawai yang digunakan dalam lengkung penentukuran taburan jisim molekul relatif: insulin, mikopeptida, glisin-glisin-tirosin-arginin, glisin-glisin-glisin
3 Instrumen dan peralatan
3.1 Kromatograf Cecair Berprestasi Tinggi (HPLC): stesen kerja atau penyepadu kromatografi dengan pengesan UV dan perisian pemprosesan data GPC.
3.2 Unit penapisan dan penyahgas vakum fasa mudah alih.
3.3 Neraca elektronik: nilai susut 0.000 1g.
4 Langkah operasi
4.1 Keadaan kromatografi dan eksperimen penyesuaian sistem (keadaan rujukan)
- 4.1.1 Lajur kromatografi: TSKgelG2000swxl300 mm×7.8 mm (diameter dalam) atau lajur gel lain daripada jenis yang sama dengan prestasi yang serupa yang sesuai untuk penentuan protein dan peptida.
- 4.1.2 Fasa mudah alih: Asetonitril + air + asid trifluoroasetik = 20 + 80 + 0.1.
- 4.1.3 Panjang gelombang pengesanan: 220 nm.
- 4.1.4 Kadar aliran: 0.5 mL/min.
- 4.1.5 Masa pengesanan: 30 minit.
- 4.1.6 Isipadu suntikan sampel: 20μL.
- 4.1.7 Suhu lajur: suhu bilik.
- 4.1.8 Untuk memastikan sistem kromatografi memenuhi keperluan pengesanan, telah ditetapkan bahawa di bawah keadaan kromatografi di atas, kecekapan lajur kromatografi gel, iaitu bilangan plat teori (N), tidak kurang daripada 10000 yang dikira berdasarkan puncak piawai tripeptida (Glisin-Glisin-Glisin).
- 4.2 Penghasilan lengkung piawai jisim molekul relatif
- Larutan piawai peptida jisim molekul relatif yang berbeza di atas dengan kepekatan jisim 1 mg/mL telah disediakan melalui pemadanan fasa bergerak, dicampurkan dalam perkadaran tertentu, dan kemudian ditapis melalui membran fasa organik dengan saiz liang 0.2 μm~0.5 μm dan disuntik ke dalam sampel, dan kemudian kromatogram piawai diperoleh. Lengkung penentukuran jisim molekul relatif dan persamaannya diperoleh dengan memplot logaritma jisim molekul relatif terhadap masa pengekalan atau melalui regresi linear.
4.3 Rawatan sampel
Timbang 10mg sampel dengan tepat dalam kelalang isipadu 10mL, tambahkan sedikit fasa bergerak, goncang ultrasonik selama 10 minit, supaya sampel larut sepenuhnya dan bercampur, dicairkan dengan fasa bergerak mengikut skala, dan kemudian ditapis melalui membran fasa organik dengan saiz liang 0.2μm~0.5μm, dan filtrat dianalisis mengikut keadaan kromatografi dalam A.4.1.
- 5. Pengiraan taburan jisim molekul relatif
- Selepas menganalisis larutan sampel yang disediakan dalam 4.3 di bawah keadaan kromatografi 4.1, jisim molekul relatif sampel dan julat taburannya boleh diperoleh dengan menggantikan data kromatografi sampel ke dalam lengkung penentukuran 4.2 dengan perisian pemprosesan data GPC. Taburan jisim molekul relatif peptida yang berbeza boleh dikira dengan kaedah penormalan kawasan puncak, mengikut formula: X=A/A jumlah×100
- Dalam formula: X - Pecahan jisim peptida jisim molekul relatif dalam jumlah peptida dalam sampel, %;
- A - Kawasan puncak peptida jisim molekul relatif;
- Jumlah A - jumlah luas puncak setiap peptida jisim molekul relatif, dikira hingga satu tempat perpuluhan.
- 6 Kebolehulangan
- Perbezaan mutlak antara dua penentuan bebas yang diperoleh di bawah syarat kebolehulangan tidak boleh melebihi 15% daripada min aritmetik bagi kedua-dua penentuan tersebut.
- Lampiran B: Kaedah untuk Penentuan Asid Amino Bebas
- Penerimaan piawaian: Q/320205 KAVN05-2016
- 1.2 Reagen dan bahan
- Asid asetik glasier: tulen secara analitikal
- Asid perklorik: 0.0500 mol/L
- Petunjuk: Petunjuk kristal ungu 0.1% (asid asetik glasier)
- 2. Penentuan asid amino bebas
Sampel dikeringkan pada suhu 80°C selama 1 jam.
Letakkan sampel dalam bekas kering untuk disejukkan secara semula jadi pada suhu bilik atau disejukkan ke suhu yang boleh digunakan.Timbang lebih kurang 0.1 g sampel (tepat sehingga 0.001 g) ke dalam kelalang kon kering 250 mL.Teruskan ke langkah seterusnya dengan cepat untuk mengelakkan sampel daripada menyerap kelembapan ambienTambah 25 mL asid asetik glasial dan gaul rata selama tidak lebih daripada 5 minit.Tambah 2 titis penunjuk kristal unguTitrasi dengan larutan titrasi piawai 0.0500 mol/L (±0.001) asid perklorik sehingga larutan berubah daripada ungu ke takat akhir.
Rekodkan isipadu larutan piawai yang digunakan.
- Jalankan ujian kosong pada masa yang sama.
- 3. Pengiraan dan keputusan
- Kandungan asid amino bebas X dalam reagen dinyatakan sebagai pecahan jisim (%) dan dikira mengikut formula: X = C × (V1-V0) × 0.1445/M × 100%, dalam formula berikut:
- C - Kepekatan larutan asid perklorik piawai dalam mol seliter (mol/L)
- V1 - Isipadu yang digunakan untuk titrasi sampel dengan larutan asid perklorik piawai, dalam mililiter (mL).
- Vo - Isipadu yang digunakan untuk titrasi blanko dengan larutan asid perklorik piawai, dalam mililiter (mL);
M - Jisim sampel, dalam gram (g).
| 0.1445: Jisim purata asid amino bersamaan dengan 1.00 mL larutan asid perklorik piawai [c (HClO4) = 1.000 mol / L]. | 4.2.3 Larutan titrasi piawai serium sulfat: kepekatan c [Ce(SO4)2] = 0.1 mol/L, disediakan mengikut GB/T601. | |
| Penerimaan piawaian: Q/70920556 71-2024 | 1. Prinsip penentuan (Fe sebagai contoh) | Kompleks besi asid amino mempunyai keterlarutan yang sangat rendah dalam etanol anhidrus dan ion logam bebas larut dalam etanol anhidrus, perbezaan keterlarutan antara keduanya dalam etanol anhidrus telah digunakan untuk menentukan kadar khelasi kompleks besi asid amino. |
| Dalam formula: V1 - isipadu larutan piawai cerium sulfat yang digunakan untuk titrasi larutan ujian, mL; | Etanol anhidrus; selebihnya adalah sama seperti klausa 4.5.2 dalam GB/T 27983-2011. | 3. Langkah-langkah analisis |
| Lakukan dua percubaan secara selari. Timbang 0.1g sampel yang dikeringkan pada suhu 103±2℃ selama 1 jam, ketepatan sehingga 0.0001g, tambahkan 100mL etanol kontang untuk melarutkannya, tapis, tapis sisa yang dibasuh dengan 100mL etanol kontang sekurang-kurangnya tiga kali, kemudian pindahkan sisa ke dalam kelalang kon 250mL, tambahkan 10mL larutan asid sulfurik mengikut klausa 4.5.3 dalam GB/T27983-2011, dan kemudian lakukan langkah-langkah berikut mengikut klausa 4.5.3 “Panaskan untuk melarutkannya dan kemudian biarkan sejuk” dalam GB/T27983-2011. Jalankan ujian kosong pada masa yang sama. | 4. Penentuan jumlah kandungan besi | 4.1 Prinsip penentuan adalah sama seperti klausa 4.4.1 dalam GB/T 21996-2008. |
4.2. Reagen & Larutan
| 4.2.1 Asid campuran: Tambahkan 150mL asid sulfurik dan 150mL asid fosforik ke dalam 700mL air dan gaul rata. | 4.2.2 Larutan penunjuk natrium difenilamina sulfonat: 5g/L, disediakan mengikut GB/T603. | 4.2.3 Larutan titrasi piawai serium sulfat: kepekatan c [Ce(SO4)2] = 0.1 mol/L, disediakan mengikut GB/T601. | |
| 4.3 Langkah-langkah analisis | Lakukan dua percubaan secara selari. Timbang 0.1g sampel, tepat sehingga 020001g, masukkan ke dalam kelalang kon 250mL, tambahkan 10mL asid campuran, selepas larut, tambahkan 30ml air dan 4 titis larutan penunjuk natrium dianilin sulfonat, dan kemudian lakukan langkah-langkah berikut mengikut klausa 4.4.2 dalam GB/T21996-2008. Jalankan ujian kosong pada masa yang sama. | 4.4 Perwakilan keputusan | Jumlah kandungan besi X1 bagi kompleks besi asid amino dari segi pecahan jisim besi, nilai yang dinyatakan dalam %, dikira mengikut formula (1): |
| X1=(V-V0)×C×M×10-3×100 | V0 - larutan piawai serium sulfat yang digunakan untuk titrasi larutan kosong, mL; | V0 - larutan piawai serium sulfat yang digunakan untuk titrasi larutan kosong, mL; | C - Kepekatan sebenar larutan piawai cerium sulfat, mol/L5. Pengiraan kandungan besi dalam kelatKandungan besi X2 dalam kelat dari segi pecahan jisim besi, nilai yang dinyatakan dalam %, dikira mengikut formula: x2 = ((V1-V2) × C × 0.05585)/m1 × 100 |
| Dalam formula: V1 - isipadu larutan piawai cerium sulfat yang digunakan untuk titrasi larutan ujian, mL; | V2 - larutan piawai serium sulfat yang digunakan untuk titrasi larutan kosong, mL;nom1-Jisim sampel, g. Ambil min aritmetik bagi keputusan penentuan selari sebagai keputusan penentuan, dan perbezaan mutlak keputusan penentuan selari tidak lebih daripada 0.3%. | 0.05585 - jisim besi ferus yang dinyatakan dalam gram bersamaan dengan 1.00 mL larutan piawai serium sulfat C[Ce(SO4)2.4H20] = 1.000 mol/L.nom1-Jisim sampel, g. Ambil min aritmetik bagi keputusan penentuan selari sebagai keputusan penentuan, dan perbezaan mutlak keputusan penentuan selari tidak lebih daripada 0.3%. | 6. Pengiraan kadar khelasiKadar khelasi X3, nilai yang dinyatakan dalam %, X3 = X2/X1 × 100Lampiran C: Kaedah untuk Penentuan Kadar Pengkelat Zinpro |
Penerimaan piawaian: Q/320205 KAVNO7-2016
1. Reagen dan bahan
a) Asid asetik glasier: tulen secara analitik; b) Asid perklorik: 0.0500mol/L; c) Petunjuk: 0.1% penunjuk kristal ungu (asid asetik glasier)
2. Penentuan asid amino bebas
2.1 Sampel dikeringkan pada suhu 80°C selama 1 jam.
2.2 Letakkan sampel dalam bekas kering untuk disejukkan secara semula jadi pada suhu bilik atau disejukkan ke suhu yang boleh digunakan.
2.3 Timbang lebih kurang 0.1 g sampel (tepat sehingga 0.001 g) ke dalam kelalang kon kering 250 mL
2.4 Teruskan ke langkah seterusnya dengan cepat untuk mengelakkan sampel daripada menyerap kelembapan ambien.
2.5 Tambah 25mL asid asetik glasial dan gaul rata selama tidak lebih daripada 5 minit.
2.6 Tambah 2 titis penunjuk kristal ungu.
2.7 Titrasi dengan larutan titrasi piawai 0.0500mol/L (±0.001) asid perklorik sehingga larutan berubah daripada ungu kepada hijau selama 15 saat tanpa mengubah warna sebagai titik akhir.
2.8 Rekodkan isipadu larutan piawai yang digunakan.
2.9 Jalankan ujian kosong pada masa yang sama.
- 3. Pengiraan dan keputusan
- Bahasa Catalan
- Physicochemical parameters
V1 - Isipadu yang digunakan untuk titrasi sampel dengan larutan asid perklorik piawai, dalam mililiter (mL).
Vo - Isipadu yang digunakan untuk titrasi blanko dengan larutan asid perklorik piawai, dalam mililiter (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
Alamat: No.147 Jalan Qingpu, Bandar Shouan, Daerah Pujiang, Bandar Chengdu, Wilayah Sichuan, China
Telefon: 86-18880477902
Produk
Mineral surih bukan organik
- Mineral surih organik
- Bahasa Swahili
- Perkhidmatan tersuai
- Pautan pantas
Profil Syarikat
| Application object | Suggested dosage (g/t full-value material) | Content in full-value feed (mg/kg) | Efficacy |
| Gujarati | Klik untuk pertanyaan | © Hak Cipta - 2010-2025: Semua Hak Cipta Terpelihara. | Peta Laman CARIAN TERBAIK Telefon |
| Tel | 86-18880477902 | Jawa | E-mel |
| 8618880477902 | Cina | Perancis | |
| Bird | Cina | Perancis | Jerman Bahasa Sepanyol |
| Aquatic animals | Bahasa Jepun | Bahasa Korea | Bahasa Arab Yunani |
| Turki | Itali | ||
| Ruminant animal g/head day | January 0.75 | Bahasa Indonesia Bahasa Afrikaans Sweden |
Poland
- Basque
- Bahasa Catalan
- Physicochemical parameters
Hindi
Lao
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
Bahasa Bulgaria
- Bahasa 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;
- Bahasa Croatia
Belanda
| Application object | Bahasa Urdu Vietnam | Content in full-value feed (mg/kg) | Efficacy |
| Gujarati | Haiti | Hausa | Kinyarwanda Hmong Bahasa Hungary |
| Piglets and fattening pigs | Igbo | Jawa | Kannada Khmer Kurdi |
| Kirgiz | Bahasa Latin | ||
| Bird | 300～400 | 45～60 | Macedonia Bahasa Melayu Malayalam |
| Aquatic animals | 200～300 | 30～45 | 1. Promote growth, improve feed conversion; 2. Improve anti-stress abolity, reduce morbidity and mortality. |
Bahasa Norway
- Pashto
- Appearance: brownish-yellow granules
- Physicochemical parameters
Bahasa Serbia
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;
Bahasa Swahili
Tajik
Bahasa Tamil
Telugu
Bahasa Thai
| Application object | Bahasa Urdu Vietnam | Content in full-value feed (mg/kg) | Efficacy |
| Bahasa Yiddish | Yoruba | Zulu | Kinyarwanda Oriya Orang Turkmen |
| 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
