20 research outputs found

    Fish side-stream as a potential peptone production: Towards zero waste fish processing

    Get PDF
    Fish processing plants generated significant side-streams composing of heads, skins, trimmings, frames, and guts, which estimated for 70-85% of raw-fish materials during fillet and surimi production. These pose a serious impact to terrestrial and aquatic environments due to the abundance of organic content. Treating side-streams, on the other hand, would impact on financial burden of the fish processing industries. Therefore, an attempt is necessary to convert fish side-streams into value-added products. This is not only to reduce financial burden but also in accordance with the 12th Sustainable Development Goal (SDG) which support zero-waste processing concept. One of the promising products from fish side-streams is peptone. Peptone, a protein hydrolysate characterized as non heat-coagulable and water-soluble product, extensively used in microbiological media. As microbial growth accelerating media, fish peptone could be a precursor for beneficial metabolic products, such as antimicrobial peptides and other bioactive compounds. This review highlights the isolation of peptone from fish processing side-streams specifically the extraction and characterization. In addition, the metabolite productions from lactic acid bacteria with fish peptone-supplemented media are also covered

    In vitro antibacterial activity of marine-derived fungi isolated from Pulau Redang and Pulau Payar Marine Parks, Malaysia against selected food-borne pathogens

    Get PDF
    Marine fungi are potential source of bioactive compounds as indicated by the increasing statistic of research findings. However similar research in Malaysia is still lacking. Hence, this study is undertaken to determine the antibacterial activity of four marine fungal isolates (PR1T4, PP2L4, PR3T13 and PR5T4) from Pulau Redang and Pulau Payar Marine Parks, Malaysia against Salmonella Typhi, Listeria monocytogenes, Staphylococcus aureus, and Escherichia coli. Fungal isolates were first macroscopically and microscopically characterized and later molecularly identified as Penicillium citrinum, Sacroladium strictum, Aspergillus sydowii and Aspergillus sp. respectively. Solid and broth fermentation of fungi were carried out to produce crude extracts and these extracts were screened for antibacterial activity. In general, solid fermentation extracts (SFE) showed significantly higher antibacterial activity (p < 0.05) against all four pathogens compared to broth fermentation extracts (BFE) as the largest inhibitory activity of SFE and BFE was (32.17±0.67 mm) and (27.57±0.81 mm) respectively both on S. aureus by S. strictum. Highest antibacterial activity against L. monocytogenes (27.95±0.81 mm) was exhibited by SFE of A. sydowii while SFE of S. strictum showed highest activity against S. aureus (32.17±0.67 mm) and E. coli (23.53±0.57 mm) and SFE of Aspergillus sp. showed largest inhibition towards S. Typhi (29.30±0.33 mm). These prominent results suggest that all four isolates have potential to be explored as new source of antibacterial agents against food-borne pathogens

    Optimization Process of the Pepsin-Solubilized Collagen from Lizardfish (Saurida tumbil Bloch, 1795) Skins by-Product

    Get PDF
    By-products from the marine fish processing are rich in organic compounds that can be converted into value-added products like collagen, and it is thought as an ideal candidate polymer for such research and medical applications. The lizardfish (Saurida tumbil Bloch, 1795) skin collagen had been investigated by our previous work, but an effective extraction method is needed to increase the yield of collagen. The purpose of this study was to optimize the method used to extract pepsin-solubilized collagen (PSC) from lizardfish skin. We employed an approach of one factor at a time (OFAT), along with response surface methodology (RSM) utilizing a central composite design (CCD), to attain the highest possible yield of the extracted collagen. Additionally, its properties were also assessed comparatively. The suggested optimal conditions for extraction were a pepsin concentration of 1.87%, a liquid-solid ratio of 24.90 mL/g, and a hydrolysis period of 38.09 h. Using these conditions resulted in a PSC yield of 21.82 g/100g, which closely matched the predicted collagen value

    Biochemical and Microstructural Properties of Lizardfish (Saurida tumbil) Scale Collagen Extracted with Various Organic Acids

    Get PDF
    The purpose of this research was to extract collagen from the scales of lizardfish (Sauridatumbil) using various acids. Acetic acid-extracted collagen (AScC) produced a higher yield (1.8 mg/g)than lactic acid-extracted collagen (LScC) and citric acid-extracted collagen (CScC) although not significantly different (p> 0.05). All extracted collagens were categorized as type I collagens with the presence of alpha chains (α1 and α2) based on the SDS-PAGE profiles. The triple-helical structure of the collagen was maintained in the AScC, LScC, and CScC as confirmed by the FTIR spectra. The UV-vis and X-ray diffraction spectra observed in all collagens were in agreement with previous work on fish scale and calfskin (commercial) collagens. The thermal stability of AScC (Tmax= 31.61◦C) was greater than LScC (Tmax= 30.86◦C) and CScC (Tmax= 30.88◦C). The microstructure of acid-extracted collagens was characterized as complex, fibrous, and multilayered, with irregular sheet-like structures.All samples were highly soluble in acidic pH (1.0–4.0) and in low concentrations of NaCl (0–20 g/L).In conclusion, the lizardfish scale collagen, particularly AScC, may be used as an alternative to terrestrial animal collagen

    Physicochemical and Microstructural Analyses of Pepsin-Soluble Collagens Derived from Lizardfish (Saurida tumbil Bloch, 1795) Skin, Bone and Scales

    Get PDF
    Reducing food waste is critical for sustainability. In the case of fish processing, more than sixty percent of by-products are generated as waste. Lizardfish (Saurida tumbil Bloch, 1795) is an economically important species for surimi production. To address waste disposal and maximize income, an effective utilization of fish by-products is essential. This study aims to isolate and characterize pepsin-soluble collagens from the skin, bone and scales of lizardfish. Significant differences (p 70%) in acidic conditions (particularly at pH 4.0) and at low sodium chloride concentrations (0–30 g/L). Microstructural analysis depicted that all extracted collagens were multi-layered, irregular, dense, sheet-like films linked by random coiled filaments. Overall, pepsin-soluble collagens from lizardfish skin, bone and scales could serve as potential alternative sources of collagens

    Microstructural and Physicochemical Analysis of Collagens from the Skin of Lizardfish (Saurida tumbil Bloch, 1795) Extracted with Different Organic Acids

    Get PDF
    Marine fish collagen has attracted considerable attention due to its characteristics, including its biodegradability, biocompatibility, and weak antigenicity, and is considered a safer material compared to collagen from terrestrial animals. The aim of this study was to extract and characterize collagen from the skin of lizardfish (Saurida tumbil Bloch, 1795) with three different acids. The yields of acetic acid-extracted collagen (AESkC), lactic acid-extracted collagen (LESkC), and citric acid extracted collagen (CESkC) were 11.73 ± 1.14%, 11.63 ± 1.10%, and 11.39 ± 1.05% (based on wet weight), respectively. All extracted collagens were categorized as type I collagen with mainly alpha chains (α1 and α2) detected and γ and β chains to some extent. Fourier transform infrared (FTIR) spectra showed an intact triple-helical structure in the AESkC, LESkC, and CESkC. UV-vis spectra and X-ray diffraction further demonstrated the similarity of the extracted collagens to previously reported fish skin collagens. AESkC (Tmax = 40.24 ◦C) had higher thermostability compared to LESkC (Tmax = 38.72 ◦C) and CESkC (Tmax = 36.74 ◦C). All samples were highly soluble in acidic pH and low concentrations of NaCl (0–20 g/L). Under field emission scanning electron microscopy (FESEM) observation, we noted the loose, fibrous, and porous structures of the collagens. The results suggest that the lizardfish skin collagens could be a potential alternative source of collagen, especially the AESkC due to its greater thermostability characteristic

    Characterizations of pepsin-soluble collagen derived from lizardfish (saurida tumbil bloch, 1795) skin, bone and scales

    Get PDF
    Reducing food waste is critical for sustainability. In the case of fish processing, more than sixty percent of by-products are generated as waste. Lizardfish (Saurida tumbil Bloch, 1795) is an economically important species for surimi production. To address waste disposal and maximize income, an effective utilization of fish by-products is essential. This study aims to isolate and characterize pepsin-soluble collagens from the skin, bone and scales of lizardfish. Significant differences (p 70%) in acidic conditions (particularly at pH 4.0) and at low sodium chloride concentrations (0–30 g/L). Microstructural analysis depicted that all extracted collagens were multi-layered, irregular, dense, sheet-like films linked by random coiled filaments. Overall, pepsin-soluble collagens from lizardfish skin, bone and scales could serve as potential alternative sources of collagens

    Biochemical analysis of collagens from the bone of lizardfish (Saurida tumbil Bloch, 1795) extracted with different acids

    Get PDF
    Background. Lizardfish (Saurida tumbil Bloch, 1795) bone is a fish by-product generated during industrial surimi processing. This by-product is an important source of collagen production since the use of terrestrial animal-based collagens no longer sought due to concern regarding the transfer of infectious diseases and religious issues. Hence, this study was carried out to determine the biochemical analysis of collagens from the bone of lizardfish extracted with different acids. Methods. Lizardfish bone collagens were extracted with various acids (i.e., acetic, lactic and citric acids). All extraction processes were conducted in a chiller room (4 ◦C). The extracted collagens were biochemically characterized, such as hydroxyproline content, Ultraviolet (UV) absorption, X-ray diffraction (XRD), Fourier transform infrared spectroscopy spectra (FTIR), Differential scanning calorimetry (DSC) and solubility in different pH values and NaCl concentrations. Results. The yield of extracted collagens ranged between 1.73% and 2.59%, with the highest (p < 0.05) observed in citric acid-extracted collagen (CaEC). Protein patterns confirmed that all-collagen samples had two identical subunits, α1 and α2, representing type I collagen. The highest whiteness value was found in acetic acid-extracted collagen (AaEC), but there was no significant difference (p ≥ 0.05) compared to lactic acid extracted collagen (LaEC). UV absorption and XRD analysis reflected the characteristics of the collagen, as reported in the literature. For the FTIR, all acid-extracted collagen samples presented a triple helical structure. The thermal transition temperature (T max = 77.92–89.04 ◦C) was in accordance with collagen extracted from other fish species. All extracted collagens were highly soluble in acidic pH and low concentrations of NaCl (0–20 g/L). In conclusion, collagens extracted from lizardfish bone may be used as alternative sources of collagen in industrial settings, and AaEC would be considered superior in terms of the characteristics evaluated in this stud

    Extraction and characterization of bioactive fish by-product collagen as promising for potential wound healing agent in pharmaceutical applications: Current trend and future perspective

    Get PDF
    Collagen is a structural protein naturally found in mammals. Vertebrates and other connective tissues comprise about 30% of an animal’s overall protein. Collagen is used in a variety of applications including cosmetics, biomedical, biomaterials, food, and pharmaceuticals. The use of marine-based collagen as a substitute source is rapidly increasing due to its unique properties, which include the absence of religious restrictions, a low molecular weight, no risk of disease transmission, biocompatibility, and ease of absorption by the body system. This review discusses recent research on collagen extraction from marine-based raw material, specifically fish by-products. Furthermore, pretreatment on various sources of fish materials, followed by extraction methods, was described. The extraction procedures for acid soluble collagen (ASC) and pepsin soluble collagen (PSC) for fish collagen isolation are specifically discussed and compared. As a result, the efficacy of collagen yield was also demonstrated. The recent trend of extracting fish collagen from marine biomaterials has been summarized, with the potential to be exploited as a wound healing agent in pharmaceutical applications. Furthermore, background information on collagen and characterization techniques primarily related to the composition, properties, and structure of fish collagen are discussed
    corecore