Hasil Pencarian  ::  Simpan CSV :: Kembali

"Lecithin is needed as a bioemulsifier product in stabilizing agents for the food, pharmaceutical and cosmetic industries due to its renewability and as it is environmentally friendly. In the food industry, most of the emulsifiers used are the oil-in-water (O/W) type. Lecithin can be seen as a promising emulsifier product because it is extracted from egg yolk and modified by enzymatic hydrolysis reaction using the papain enzyme. This modification will change the molecular structure of the compound, which makes lecithin more stable in the oil-in-water type of emulsion. This study aims to determine the optimum amount of papain enzyme used in the hydrolysis reaction to achieve the most stable O/W lecithin emulsion type. The results show that the breaking of a single fatty acid chain from the structure of lecithin can be demonstrated by FTIR instrumentation. The fatty acids detected from the lecithin structure are shown at wavenumber 1699.45 cm-1 (C=O), 1231.44 cm-1 (C-O), 1422.45 cm-1 (C-O-H), 1092.85 cm-1 (C-C), 665.89 cm-1 (CH2), and 3400.57 (-OH in carboxylate). Determination of the modified lecithin yield was made by several tests, namely a stability test, and tests for acid value, surface tension and zeta potential. From the results of tests, the emulsion stability for the O/W type was achieved in modified-lecithin using a 4% papain enzyme dosage, with a stability duration of up to 31 hours. The lowest acid number was achieved in modified-lecithin using a 2% papain enzyme dosage with value of 10.40. The lowest surface tension was obtained in modified-lecithin using a 2% papain enzyme dosage with a surface tension value of 48.68 dyne/cm. The zeta potential of the modified-lecithin using a 2% papain enzyme had a value of -94.8 mV. These results show that the enzymatic hydrolysis of lecithin using a papain enzyme is clearly able to enhance the emulsifier properties of the lecithin produced."

"ABSTRAKKoagulasi adalah metode yang digunakan untuk menggumpalkan daging. Agen koagulan yang digunakan adalah enzim papain, transglutaminase dan rennin. Enzim papain tergolong protease sulhidril. Pada penggumpalan daging apabila dikenakan enzim papain maka terjadi reaksi pemutusan ikatan peptide sehingga protein terpotong-potong membentuk rantai yang lebih pendek. Komposisi penambahan agen koagulan yang dilakukan adalah 6 ml untuk setiap 100 gram daging ikan lele gerusan. Berdasarkan hasil penelitian, diketahui nilai-nilai untuk koagulasi menggunakan agen enzim papain, enzim transglutainase dan enzim rennin secara berurutan adalah kadar protein (16,01%; 16,03%; 17,21%), kadar air (72,44%; 70.98%, 72,5%), kadar serat kasar (0,4%; 0,56%; 0,29%) kadar lemak (7,88%; 7,75%; 8,85%), kadar karbohidrat (0,68%; 1,61%; 0,32%). Kemudian diketahui bahwa enzim transglutaminase paling baik dalam peran sebagai agen koagulan dibanding enzim lainnya. Diketahui transglutaminase memiliki kinerja lebih baik dalam menggumpalkan daging ikan lele, meskipun dikonsikan pada suhu 800C.

---

ABSTRACTCoagulation is the method used to agglomerate meat. Coagulant agents used are papain, transglutaminase and rennin enzymes. Papain enzymes are classified as protease sulhydryl. In agglomeration of flesh when it is enriched papain enzyme then the peptide bond termination reaction occurs so that the protein is cut into shorter chains. The composition of the addition of coagulant agent is 6 ml for every 100 grams of scalloped catfish meat. Based on the results of the research, it is known that the values ​​for coagulation using papain enzyme agent, transglutainase enzyme and rennin enzyme are protein content (16,01%; 16,03%; 17,21%), moisture content (72,44%; 70.98%, 72.5%), crude fiber content (0.4%, 0.56%, 0.29%) fat content (7.88%, 7.75%, 8.85%), carbohydrate 0.68%; 1.61%; 0.32%). Then it is known that transglutaminase enzyme is best in the role of coagulant agent than any other enzyme. Known transglutaminase has better performance in catfish flesh, although dikonsikan at a temperature of 800C."

"ABSTRAKPapain adalah enzim protease pemecah protein yang terdapat pada getah pepaya yang berfungsi sebagai katalis reaksi pemecahan rantai polipeptida pada protein dengan cara menghidrolisis ikatan peptidanya menjadi senyawa yang lebih sederhana seperti asam amino. Dalam penelitian ini papain dikembangankan menjadi bahan aktif sediaan sabun padat dalam bentuk enzim papain kasar crude untuk membersihkan kulit manusia dari kotoran yang mengandung protein. Untuk memperoleh khasiat lain dilakukan penambahan bahan aktif yaitu antioksidan dari buah pepaya murni. Penelitian ini bertujuan untuk menghasilkan formula sabun padat yang aman untuk kulit dengan memenuhi standart SNI 1996 serta teruji manfaat dalam penambahan enzim papain kasar dan mengetahui aktivitas antioksidan sabun. Enzim papain kasar dan antioksidan dari buah pepaya akan diformulasikan menjadi sabun sediaan padat menggunakan metode saponifikasi. Formula terbaik dengan nilai pH 10,35; jumlah asam lemak 79 ; kadar alkali bebas 0,108; bobot jenis 1,0595; stabilitas busa t5menit 78 dan t30menit 33 ; dan nilai IC50 13.657 ppm dilakukan uji manfaat pengangkatan kotoran terhadap sabun tanpa enzim. Hasilnya perbedaan persen kotoran terangkat antara sabun negatif dengan enzim terhadap kontrol positif tanpa enzim menggunakan spektrofotometer UV-VIS adalah 9 pada t10menit, dan menggunakan pengukuran massa substrat perbedannya adalah 4 pada t10menit.

---

ABSTRACTPapain is protease enzyme breaking protein that can be found in latex of papaya which acts as a reaction catalyst breaking polypeptide chain of protein by hydrolyzing the peptide bonds into simpler compound like amino acid. The enzyme is able to break down organic molecules made of amino acids, known as polypeptides. In this study papain developed into active ingredients of solid soap preparations in the form of crude papain enzymes to cleanse human skin. This study aims to produce a solid soap formula that is safe for the skin by meeting the standards of SNI 1996 and tested the benefits in the addition of rough papain enzymes. Crude papain enzymes and antioxidants from papaya fruit will be formulated into solid soap preparations using saponification methods. The best formula with value of pH 10.35 Amount of fatty acid 79 Free alkali content of 0.108 Weights type 1.0595 Foam stability of t5menit 78 and t30menit 33 And IC50 13,657 ppm value was tested the benefit of removal of dirt to soap without enzyme. The difference in percentage of dirt lifted between control negative with enzyme and control positive without enzyme soap using UV VIS spectrophotometer was 9 in t10 min, and using the substrate mass measurement was 4 in t10 min."