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Articles by Retno Indrati
Total Records ( 5 ) for Retno Indrati
  Ita Zuraida , Sri Raharjo , Pudji Hastuti and Retno Indrati
  Background and Objective: Differences in gelling properties may be attributed to the chemical composition and setting conditions at a particular temperature employed during the formation of surimi gels. The aim of this study was to investigate the chemical composition and effect of setting condition on the gel properties of surimi prepared from Clarias gariepinus (local name "lele dumbo"). Materials and Methods: Kamaboko gel was prepared by incubating the surimi sol at 35°C prior to heating at 90°C, while directly heated gel was prepared by heating the sol at 90°C. Data were subjected to analysis with a one-way ANOVA for comparison of means at a 5% level of significance. Results: The myofibrillar and sarcoplasmic protein contents were 16.27±0.23 and 2.02±0.06 mg N g–1 surimi, respectively. About 40% of transglutaminase activity was retained in the final surimi. Kamaboko gel showed higher gel strength, hardness and springiness when compared with directly heated gel. However, it had a lower expressible moisture content. Both surimi gels showed no significant difference in the whiteness parameter. Electrophoretic patterns indicated that although myosin heavy chain may undergo polymerisation in both, kamaboko gel and directly heated gel, the extent of polymerisation may be greater in kamaboko gel. Conclusion: The two-step heating involving setting of surimi sol at 35°C prior to heating at 90°C could enhance gel properties of lele dumbo surimi.
  Suryanti , Retno Indrati , Hari Eko Irianto and Djagal Wiseso Marseno
  Methods of gelatin extraction from nila fish (Oreochromis nilotichus) skin were studied using acid treatment (acetic acid or citric acid) at various concentrations (0, 0.05, 0.10, 0.15, 0.20 and 0.25 M) and soaking times (0, 1, 2, 3, 4 and 5 h). Gelatin extracted from nila skin treated with 0.10 M acetic acid for 2 h produced the highest yield (25.33%) with a gel strength of 346.16 g bloom and a molecule size distribution of 38-241 kDa. Gelatin extracted from the skin treated with 0.05 M citric acid for 1 h resulted in a yield of 21.09% with a gel strength of 134.52 g bloom and a molecule size distribution of 23-145 kDa. Gelatin extracted by both acids had similar infra-red absorbance spectra, ranging from 1640 to 1239 cm-1. However, gelatin from nila skin treated with 0.10 M acetic acid for 2 h produced gelatin with a more homogenous molecular microstructure than nila skin treated with 0.05 M citric acid for 1 h.
  Ita Zuraida , Sri Raharjo , Pudji Hastuti and Retno Indrati
  Background and Objective: The properties of surimi gel are influenced by the fish species used to generate the gel, their chemical compositions and the endogenous enzymatic activity in fish muscle. The aim of this research was to investigate the potential of Clarias gariepinus (local name "lele dumbo") as an alternative raw material for surimi production based on proximate composition, amino acid profile, protein composition and transglutaminase (TGase) and protease activity. Materials and Methods: This study used lele dumbo muscle as the raw material. The chemical properties of proximate composition, amino acid profile, protein composition and endogenous enzyme activity of the sample were determined using standard methods with three replicates. The results were presented as the means±standard deviation. Results: The moisture, ash, crude protein and crude fat content of fish muscle were 73.01±0.05, 0.78±0.02, 16.08±0.03 and 2.03±0.05%, respectively. The lele dumbo muscle has glutamine and lysine residues that can support TGase activity. Myofibrillar proteins were found as the major protein compounds in the fish muscle (16.57±0.03 mgN g–1 muscle) and the sarcoplasmic and stromal protein contents were lower, 4.38±0.03 and 0.71±0.05 mgN g–1 muscle, respectively. The TGase activity of the fish muscle was 0.18 U mL–1 (ΔAbs. = 0.21), which was higher than the protease activity (ΔAbs. = 0.10). Conclusion: Lele dumbo is a potential alternative raw material for surimi production.
  Bagus Fajar Pamungkas , Supriyadi , Agnes Murdiati and Retno Indrati
  Background and Objective: The optimal use of haruan scales for preparing collagen is a promising method to increase value-added products and to protect the environment. The aim of this research was to characterize the acid- and pepsin-soluble collagens from haruan (Channa striatus) scales. Materials and Methods: The fish scales were subjected to an extraction with 0.5 M acetic acid and a digestion with 0.1% pepsin. The results are presented as the mean±standard deviation. Results: The yields of the acid-soluble collagen in the haruan scales (ASC-SH) and the pepsin-soluble collagen in the haruan scales (PSC-SH) were 1.44 and 2.94% (on a dry basis), respectively. ASC-SH and PSC-SH contained glycine as the major amino acid and had high imino acid contents (238 and 242 residues/1,000 residues, respectively). Based on the SDS-PAGE pattern, both ASC-SH and PSC-SH were identified as type I collagens containing α1 and α2 chains. β and γ components were also found in both collagens. The FTIR spectra indicated that both collagens had triple helical structures. The collagens were both soluble at acidic pH levels (1-4) and their solubility was low when the NaCl concentrations were above 3% (w/v). Conclusion: It was concluded that haruan scales could be an alternative source of collagen and that the characteristics of the collagens were slightly affected by the extraction process used in this study.
  Endah Puspitojati , Muhammad Nur Cahyanto , Yustinus Marsono and Retno Indrati
  Background and Objective: Angiotensin-converting enzyme (ACE) inhibitory peptides from various food sources have been studied extensively. We are interested in studying the inhibition of ACE from fermented tempe made from the jack bean, which is a commonly used source of plant-based protein. The purpose of this study was to determine the optimal incubation period for the production of peptides with high ACE inhibitory activity. Materials and Methods: After soaking and boiling, the jack beans were inoculated with tempe inoculum and incubated for 0-120 h. During the incubation, various parameters, such as proteolytic activity, peptide content, hydrolysis degree, protein pattern and ACE inhibition, were monitored. All the parameters were measured using standard methods. Results: Tempe fermentation caused hydrolysis of the jack bean protein, producing soluble high molecular weight proteins (from previously insoluble) and protein fragments (monitored from SDS PAGE data). The highest protein hydrolysis occurred after 96 h fermentation period, which were observed from the highest proteolytic activity (25.39 units g–1), hydrolysis degree (19.85%) and peptide content (6.05 mg mL–1). The highest ACE inhibitory activity did not coincide with the highest levels of protein hydrolysis but rather were obtained after 72 h of tempe fermentation (IC50 = 1.03 mg mL–1). Conclusion: Jack bean tempe is a potential source of ACE inhibitory peptides, the highest ACE inhibitory activity occurred after 72 h of incubation.
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