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The current objective was framed on isolation of two angiotensin-I converting enzyme inhibitory peptides from coastal trashes of squilla muscle (Harpiosquilla raphidea) prepared by enzymatic hydrolysis using alcalase, thermolysin and trypsin, which showed the highest degree of hydrolysate in 12th h hydrolysate 87.9 ± 1.6%, 63.1 ± 1.1% and 91.1 ± 2.7% respectively. Among these three hydrolysates, alcalase 5th h (64.8 ± 0.3) and thermolysin 6th h (68.4 ± 1.0) found to be maximum ACE-I inhibition activity. Initial separation was performed by ultra filtration (10–3 kDa) into three different fractions, alcalase (below 3 kDa) fraction observed maximum ACE-I inhibition activity with 75.2 ± 3.5% and thermolysin (3–10 kDa) with 79.5 ± 1.0% inhibition. Further, these two fractions have taken to ion exchange and gel filtration chromatography, the identified ACE-I inhibitory fractions (AC-A2 and TH-A2) also examined for its antioxidant properties. Further, these fractions were determined to be non-toxic against cell lines, functional activities by various assays and characterized into tri peptides MSN (Met-Ser-Asn) and MTH (Met-Thr-His) with a molecular weight of 350 Da and 388 Da respectively using LC–MS/MS. These low molecular weight peptides from natural sources may act as potential ingredient for nutraceutical and pharmaceutical industries.

The visceral mass of the gastropod, Harpa ventricosa was hydrolysed using trypsin, alcalase and pepsin for 12 h to produce protein hydrolysates. Subsequently, the active hydrolysate was observed in the 3rd hour of tryptic hydrolysate (29.17 ± 0.62 and 34.85 ± 0.55 %) using human red blood cell (HRBC) membrane stabilization and albumin denaturation (AD) assays. The active hydrolysate was fractionated by membrane filtration unit, where

Gelatin was extracted from 3 (body, foot, and viscera) different body parts of Ficus variegata using an alkaline treatment. Composite scaffolds were prepared for tissue engineering applications. Proximate analysis of F. variegata prior to extraction showed percentage values of 16.67–14.33% for protein, 74.53–72.72% for moisture, 3.63–2% for ash, and 2.33–0.33% for lipids. Extracted gelatin was characterized using Fourier transform infrared (FTIR), SDS-PAGE, and amino acid analysis. Composite scaffolds using alkali treated gelatin of all 3 body parts with 4 different commercial cross-linkers [chitosan, hydroxy apatite (HA), glutaraldehyde, and nano hydroxy apatite (nHA)] were prepared and structural morphology and porosity were analyzed using scanning electron microscopy (SEM). The nHA blended gelatin scaffolds had a pore size ranging 1–10 μm. The swelling ratio, in vitro degradation, and the protein adsorption capacity was observed to be high in chitosan blended gelatin scaffolds.

In the present study, northern whiting fish (Sillago sihama) muscle was hydrolyzed with gastrointestinal enzymes (pepsin, trypsin and α-chymotrypsin) separately and the resulted protein hydrolysates were tested for antioxidant activities using DPPH radical scavenging activity and reducing power assays. The protein hydrolysate obtained from trypsin exhibited highest antioxidant activity. Further, it was fractionated by consecutive chromatography using anion exchange and gel filtration chromatography; the separated fractions were collected and evaluated for antioxidant activity. The results showed that fraction 2 exhibited high chelating activity (73.15 % at 0.5 mg/mL) and best radical scavenging activity for DPPH radical (55.16 % at 0.5 mg/mL), ABTS radical (57.98 % at 50 μg/mL), superoxide radical (39.55 % at 200 μg/mL) and hydroxyl radical (51.33 % at 100 μg/mL). In addition, the active fraction showed strong antioxidant activity in the inhibition of linoleic acid autooxidation (60 % at 0.5 mg/mL) and also it exhibited significant protective effect on DNA damage caused by hydroxyl radicals. The size of the active fraction was found to be

The objective of this study was to determine the physicochemical and nanostructural properties of the alkali pre-treated gelatin from 3 different body parts (skin, muscle, and bone) of cornet fish (Fistularia petimba). The maximum yield of protein and viscosity was obtained in bone than other parts and Fourier transform infrared (FTIR) spectroscopy was carried out to characterize the extracted gelatin. Prior to extraction, the proximate composition was investigated clearly and the percentage of protein (15.50–29%), ash (4.32–6.50%), moisture (71.85–79.20%), and lipid (0.36–1.38%) content were estimated. Morphology of alkaline gelatin extracted from skin, muscle, and bone were studied using atomic force microscopy (AFM). The AFM images represented the scanning was done at 1.9 μm, 510, and 110 nm for skin, muscle, and bone, respectively showed the separate individual aggregates and the nano size particles of 0.17 μm, 100, and 219 nm, respectively. Amino acids like glycine, proline, and hydroxyproline were found with highest level in all the body parts of the extracted gelatin using HPLC.

Type I collagen was extracted from the bone of two marine fishes; Magalaspis cordyla and Otolithes ruber and its efficacy in wound healing was studied. The yields of acid soluble (30.5 and 27.6%) and pepsin soluble (45.1 and 48.6%) collagen were respectively as per their dry weight basis. Extracted protein was characterized as type I collagen basing on SDS PAGE, UV–Vis, FTIR spectrometer and amino acid composition. The characterized collagen was cross-linked with glutaraldehyde and found to possess three dimensional pores and acted efficiently in healing the excision wounds made on Wistar rats. Bone is generally considered as waste and discarded in many processing plant. But, the current study proved that it has excellent medicinal importance and reveals a possible way to convert this waste into a medicinally important source.

To make more effective use of available marine resources, acid soluble collagen (ASC) was isolated from body and foot of wedge clam Donax cuneatus Linnaeus, 1758 with acetic acid and was characterized for their potential and commercial applications. The yield of ASC was 17% and 23% respectively. SDS PAGE, UV and FTIR spectroscopy showed that both were type I mainly with slight differences. HPLC was used for identifying the presence of different types of amino acids, where glycine was more or less 20% in both the samples and takes the lead amino acid position and presence of imino acids (11.8 and 12.6%) has been the characteristic feature of type I collagen.

The current study aims at the isolation and characterization of the peptides, believed to have antioxidant activity, from Conus betulinus by using different types of enzymes. The body and viscera of C. betulinus were treated with three enzymes viz. trypsin, pepsin and papain to obtain peptide hydrolysates. The activities of the hydrolysates were analyzed by DPPH and hydroxyl radical assay by using electron spin resonance (ESR) device. Active hydrolysates were purified using ion exchange chromatography followed by gel filtration chromatography. The activity of the separated fractions was analyzed by ESR; in which the result showed that trypsin hydrolysate of body (28.48 and 76.00%) and viscera (38.45 and 83.00%) respectively have high activity than the other hydrolysates. The HPLC result of purified fraction showed, presence of active amino acids viz., metheonine, cystine, histidine etc. This purified peptide has more antioxidant activity that could reduce the excess free radicals in body in order to prevent free radical induced diseases.

We have investigated the antioxidant activity of protein hydrolysates prepared from backbones of two commercially important fishes; seela (Sphyraena barracuda) and ribbon fish (Lepturacanthus savala). Pepsin and trypsin hydrolysates were found more potent to inhibit lipid peroxidation in case of ribbon and seela fish respectively and were further purified by using fast protein liquid chromatography on anion exchange and gel filtration chromatography. The active peaks after gel filtration chromatography of seela fish was able to scavenge 2,2-diphenyl-1-picryhydrazyl and hydroxyl radicals by 61 ± 2.3 and 58.7 ± 2.3% and ribbon fish hydrolysate by 60.0 ± 2.6 and 55.6 ± 1.8% as measured by ESR spectroscopy. And the active fractions showed presence of both essential and non-essential amino acids with high percentages of arginine (11.95 and 12.76%) and lysine (13.49 and 13.89%).

The sulphated polysaccharide from the widespread Tridax procumbens plant was studied for the anticoagulant, antiherpetic and antibacterial activity. The anticoagulant activity was determined by the activated partial thromboplastin time assay. The sulphated polysaccharide from T. procumbens represented potent anticoagulant reaching the efficacy to heparin and chondroitin sulphate. Moreover, the sulphated polysaccharide extracted from T. procumbens was found non-toxic on Vero cell lines up to the concentration of 200 μg/ml. Sulphated polysaccharide exhibited detectable antiviral effect towards HSV-1 with IC(50) value 100-150 μg/ml. Furthermore, sulphated polysaccharide from T. procumbens was highly inhibitory against the bacterial strains Vibrio alginolyticus and Vibrio harveyi isolated from oil sardine.

The antioxidant activity of marine clam, Meretrix casta (Chemnitz) protein hydrolysates prepared from different organs (body, foot and viscera), using the commercial enzymes (pepsin, trypsin and papain) were determined. The protein hydrolysate had a high antioxidant activity where, pepsin hydrolysate of viscera and trypsin hydrolysate of body and foot showed good activity. The viscera pepsin hydrolysate and foot trypsin hydrolysates were purified using FPLC on ion exchange and gel filtration chromatography procedure and activity was determined by DPPH radical scavenging and reducing ability assays. Further the amino acid content of the purified fractions was analyzed using HPLC. Active fractions contained good quantity of both essential and non-essential amino acids.