Peer Reviewed Journal Articles (Inter.) (FP)

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    Characteristics and seal ability of blend films based on chicken protein isolate and fish skin gelatin
    (Springer, 2021-10-11) Nilsuwan,Krisana; Arnold, Marcellus; Benjakul, Soottawat; Prodpran, Thummanoon; Koro de la Caba; C. O., Mohan
    Blend films from chicken protein isolate (CPI) and fish skin gelatin (FSG) at various CPI/FSG ratios (100:0, 80:20, 70:30, 60:40, 0:100), prepared at pH 3 or 11 were characterized. At the same pH, tensile strength (TS) of CPI/FSG films was higher than CPI and FSG films, and CPI/FSG film (60:40) had highest TS. Moreover, elongation at break (EAB) of blend films increased as FSG content augmented. EAB of CPI film and CPI/FSG (80:20) film was similar for both pHs. CPI films generally possessed higher water vapor permeability (WVP), light barrier property and b*-value than FSG counterpart. CPI films prepared at both pHs were not sealable. Nevertheless, addition of FSG improved sealing ability of blend films. At the same CPI/FSG ratio, seal strength and seal efficiency were lower for films prepared at pH 11. Moreover, higher TS and b*-value were gained, compared to those of films prepared at pH 3. Less cracks on surface and cross-section appeared for CPI/FSG films as revealed by scanning electron microscopy images, compared to CPI and FSG films. Therefore, incorporation of FSG up to 40% into blend film was able to improve mechanical properties, WVP, and sealing ability of blend films.
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    Antioxidant properties of papain mediated protein hydrolysates from fresh water carps (Catla catla, Labeo rohita and Cirrhinus mrigala) and its application on inhibition of lipid oxidation in oil sardine mince during ice storage
    (Springer, 2021-03-12) Krishnamoorthy, Elavarasan; Bangalore Aswathnarayan Shamasundar
    Fish protein hydrolysates (FPH) from fresh water carps Catla catla, Labeo rohita and Cirrhinus mrigala were prepared with 5, 10, 15 and 20% degree of hydrolysis (DH) using papain enzyme. FPH were evaluated for antioxidant properties using in vitro assays such as DPPH free radical scavenging activity (at 10 mg/ml), ferric reducing antioxidant power assay (at 20 mg/ml) and linoleic acid peroxidation inhibition activity (at 10 mg/ml). Antioxidant properties of FPH varied with species and DH. The DPPH radical scavenging activity, linoleic acid peroxidation inhibition activity and ferric reducing antioxidant power (as absorbance at 700 nm) of FPH from carps was in the range of 59–92%, 52–85% and 0.388–0.663 respectively. Based on the overall antioxidant activity, FPH from C. catla with 20% DH was added to oil sardine mince at different concentration (0.1, 0.2 and 0.4%) and found to inhibit effectively the formation of peroxides and malonaldehyde in dose dependent manner. FPH from C. catla with 20% DH was fractionated using size exclusion chromatography and had three different peptide fractions with the approximate molecular weight of 6561–2106 Da (fraction 1), 1942–994 Da (fraction 2) and 935–383 Da (fraction 3). The present study showed promising results that the fish protein hydrolysates from fresh water carps muscle proteins can be used as natural antioxidants in food system. Production of fish protein hydrolysates with nutraceutical properties could be the way forward for better utilization and value addition.
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    Characterization of chitin extracted from enzymatically deproteinized Acetes shell residue with varying degree of hydrolysis
    (Elsevier, 2021) Dhanabalan, Vignaesh; K.A., Martin Xavier; Eppen, Shibu; Joy, Adharsh; Balange, Amjad; K.K., Asha; L., Narasimha Murthy; Bhusan Nayak, Binaya
    Acetes shrimp is an unexploited tiny shrimp mainly landed as bycatch which is a good source for the recovery of protein and chitin. In the present study, the residual shell obtained after the hydrolysis of Acetes was used for the extraction of chitin by combining enzymatic and chemical treatments. Enzymatic hydrolysis with Alcalase was performed at different rates. Results showed that the protein removal efficiency increases with the increase in DH and the maximum deproteinzation was achieved at 30 % DH (93.68 %). The FTIR spectra showed two sharp bands for chemically prepared chitin and 30 % DH chitin at 1627–1629 and 1664􀀀 1665 cm􀀀 1 indicating that its alpha amorphous structure. The degree of N-acetylation was found to be higher in enzymatically prepared chitin in all different hydrolytic treatment rather than chemically prepared. The surface morphologies of chitin revealed the porous and nanofibrous structures for 30 % DH chitin and chemically prepared chitin.
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    Microencapsulation of bixin pigment by spray drying: Evaluation of characteristics
    (LWT - Food Science & Technology, 2021-06) M., Balakrishnan; S., Gayathiri; P., Preetha; R., Pandiselvam; G., Jeevarathinam; D. S., Aniesrani Delfiya; Anjineyulu, Kothakota
    The present work was conducted to microencapsulate the commercial (CE), and solvent (SE) extracted annatto using modified starch (MS) and gelatine (G) blend as wall material by spray drying. The conditions used were solid: liquid (S/L) ratio 1:10, extraction temperature 70 ◦C, and extraction time interval (10–35 min) for the SE annatto extract. Among the different treatments, 20 min extraction time was highly significant in the recovery of 93.19 ± 0.06 g/100 g of annatto seeds of total pigment and 94.78 ± 0.89% of bixin recovery. Both SE and CE annatto extracts have been used as a core material with wall materials (MS: G) in varied ratios of 100:0 to 60:40 to produce the microcapsules. The highest encapsulation efficiency of 86.18% and 86.37% were recorded for the SE and CE microcapsules prepared with the wall material (MS: G) ratio of 60:40. Encapsulated extract recorded higher stability against light, oxygen, and heat than the non-encapsulated annatto. In vitro release study of both microcapsules in three different pH conditions (1.2, 6.8, and 7.4) revealed an initial burst release of bixin pigment followed by a controlled release of bixin from microcapsules.
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    Exploiting of Secondary Raw Materials from Fish Processing Industry as a Source of Bioactive Peptide-Rich Protein Hydrolysates
    (MDPI, 2021) Gajanan Phadke, Girija; Rathod, Nikheel Bhojraj; Ozogul, Fatih; Elavarasan, Krishnamoorthy; Karthikeyan, Muthusamy; Kyung-Hoon Shin; Se-Kwon Kim
    Developing peptide-based drugs are very promising to address many of the lifestyle mediated diseases which are prevalent in a major portion of the global population. As an alternative to synthetic peptide-based drugs, derived peptides from natural sources have gained a greater attention in the last two decades. Aquatic organisms including plants, fish and shellfish are known as a rich reservoir of parent protein molecules which can offer novel sequences of amino acids in peptides, having unique bio-functional properties upon hydrolyzing with proteases from different sources. However, rather than exploiting fish and shellfish stocks which are already under pressure due to overexploitation, the processing discards, regarded as secondary raw material, could be a potential choice for peptide based therapeutic development strategies. In this connection, we have attempted to review the scientific reports in this area of research that deal with some of the well-established bioactive properties, such as antihypertensive, anti-oxidative, anti-coagulative, antibacterial and anticarcinogenic properties, with reference to the type of enzymes, substrate used, degree of particular bio-functionality, mechanism, and wherever possible, the active amino acid sequences in peptides. Many of the studies have been conducted on hydrolysate (crude mixture of peptides) enriched with low molecular bioactive peptides. In vitro and in vivo experiments on the potency of bioactive peptides to modulate the human physiological functions beneficially have demonstrated that these peptides can be used in the prevention and treatment of non-communicable lifestyle mediated diseases. The information synthesized under this review could serve as a point of reference to drive further research on and development of functionally active therapeutic natural peptides. Availability of such scientific information is expected to open up new zones of investigation for adding value to underutilized secondary raw materials, which in turn paves the way for sustainability in fish processing. However, there are significant challenges ahead in exploring the fish waste as a source of bioactive peptides, as it demands more studies on mechanisms and structure–function relationship understanding as well as clearance from regulatory and statutory bodies before reaching the end user in the form of supplement or therapeutics.