Malaysian Mahseer (Tor spp.) is a highly priced native freshwater fish in Malaysia and much sought after as food, ornamental and recreational fish. However, the production of mahseer is still insignificant. Due to the decline in the wild stock population of mahseer, farmers are compelled to rely heavily on imported broodstock or hatchery-produced fingerlings. The R&D on mahseer is also limited with only several reports on breeding techniques, feed requirement and genetic distance between populations. The availability of superior breeding stocks, efficient hatcheries management and formulation of maturation diet that could expedite the maturation process could greatly assist in increasing mahseer aquaculture productivity. This paper presents the R&D carried out by the Fisheries Research Institute, Department of Fisheries Malaysia starting from the 11th Malaysia Plan (2016 to 2020), particularly on the broodstock development, breeding, disease, seed management, formulation and validation of maturation diet. In this programme, broodstocks obtained from five different states namely Pahang, Johor, Sarawak, Perak and Terengganu, Malaysia were used as a base population and mated using full diallel method to produce a total of 75 families. The maturation diet enhanced the breeding capacity and shortened the maturation period of mahseer from 3.0 years to only 1.8–2.0 years. Three innovations, hatching system, nursing system and maturation diet were produced from this programme were also registered innovations. This paper also deliberates the challenges faced in broodstock development programme and the way forward.
A fish kill incident was reported at the marine fish culture areas north of Perak and south of Penang, Malaysia, on 26 May 2020. An investigation was carried out at 10 stations in Kerian, Perak and Seberang Perai Selatan, Penang. Seawater samples were collected to identify microalgae species and determination of dissolved inorganic nutrients. The physical parameters of water such as salinity, pH, temperature and dissolved oxygen were measured in situ while the dissolved inorganic nutrients were analysed spectrophotometrically. The dominant microalga was identified as Margalefidinium fulvescens (Iwataki, Kawami & Matsuoka) Gómez, Richlen & Anderson, 2017, based on the morphological and molecular characterisation of the large subunit ribosomal gene. Long rounded and ellipsoidal cells, 30-43 µm in length, appeared in chains of single, two, four or eight cells. The sulcus was slightly narrow surrounding the cell about one turn, but the cingulum was rather deep, encircling the cell approximately twice, and the chloroplasts were brownish, granular and scattered peripherally. The highest M. fulvescens cell counts were recorded at 6.22 × 105 cells L-1 and 4.61 × 105 cells L−1 in Kerian, Perak and Seberang Perai Selatan, Penang, respectively. The physical parameters of the seawater from the affected sites were within the Malaysian Marine Water Quality Standard (MMWQS) for aquaculture. However, slightly higher levels of nitrate, phosphate and ammonia were noted at several stations. Although the exact cause of the bloom was undecided, it could be due to nutrient discharge along the coasts, which also concurred with the transition phase of the northeast to the southwest monsoon.
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 < 0.05) in the yields of collagen were noted with the highest yield recorded in pepsin-soluble skin collagen (PSSC) (3.50 ± 0.11%), followed by pepsin-soluble bone collagen (PSBC) (3.26 ± 0.10%) and pepsin-soluble scales collagen (PSCC) (0.60 ± 0.65%). Through SDS−polyacrylamide gel electrophoresis, the presence of two alpha chains were noted and classified as type I. From Fourier transform infrared spectroscopy (FTIR) analysis, the triple-helix structure of the collagen was maintained. The X-ray diffraction and UV visible spectra characteristics of the lizardfish collagens in this study are similar to the previously reported fish collagens. In terms of thermostability, PSSC (Tmax = 43.89 °C) had higher thermostability in comparison to PSBC (Tmax = 31.75 °C) and PSCC (Tmax = 30.54 °C). All pepsin-soluble collagens were highly soluble (>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.
Abstract By-product removal in fish processing is estimated to be between 25 and 70% due to improper fish production handling and significant problems in the fish industry today. Therefore, one of the ways to manage the raw material of by-product is through protein hydrolysis. However, one of the most effective methods for managing this raw material, which includes skin, bones, heads, and viscera, is to convert their protein into peptides via hydrolysis methods, resulting in fish protein hydrolysate (FPH). FPH has been shown to have bioactive properties such as antibacterial, antihypertensive, antioxidative, anticancer, and anticoagulant properties. Bioactivity could be fully utilised in the future in both the nutraceutical and food industries. Numerous studies have been published on the acceptability of FPH in obtaining bioactive properties from various fish, particularly antibacterial activity. For example, the antibacterial peptide was identified as FPIGMGHGSRPA, consisting of 12 amino acids. Its antibacterial activity was tested against B. subtilis using 800 g/mL ampicillin. The inhibition zone increased with peptide concentration. This review discusses functional bioactive peptides derived from fish protein hydrolysate that can be used as antibacterial agents by inhibit Gram-positive and Gram-negative bacterial growth. It also covers fish species, parts, and hydrolysis methods to maximise yields.
Lately, Muslim consumers in Malaysia, are avoiding catfish (Clarias gariepinus) owing to the uncertainty of its halal status. This is due to the use of unclean/impure substances (najasa in Islamic law) as feed from animal carcasses or feed incorporated with animal waste (fat, blood or bone). Under the islamic law, animals which consume large quantities of najasa and led to noticeable changes of its odour, colour and taste of the meat are haram (forbidden) or makruh (undesirable). To our knowledge there is no investigation on whether the feed could alter the odour, taste or colour of the catfish from this perspective. Thus a study was undertaken to evaluate if feeding diets comprising of najasa will affect the nutritional composition and sensory characteristics of catfish.The fish were fed with imported pellets (consisting of 10-15% blood meal with porcine DNA detected), local pellets and 100% chicken offal for 12 weeks. The results showed treatment with imported pellets do not have a significant (p>0.05) effect on the nutritional composition (proximate composition, amino acids and fatty acids profiles), colour, odour and flavour of catfish fillet, but significantly (p<0.05) change the odour and flavour.
Converting skin by-product of unicornfish (Naso reticulatus Randall, 2011) into a valuable commodity like collagen is a good strategy to explore alternative sources for land-based animals. Additionally, marine fish collagens are preferable due to their safer and great properties. This project aimed to compare extractability of collagens prepared with three organic acids (i.e., acetic, lactic and citric acids), and their characteristics were also discussed. Collagen extracted with citric acid (CSCUS) (7.10%) had a significantly higher yield (p
Antimicrobial resistance (AMR) is a serious and growing global public health threat.Given the grave importance of AMR, the United Nations General Assembly has called for the development and implementation of the national action plans (NAP) on AMR in each of its member countries.The Malaysia NAP was launched in February 2017 with collaborative approach from Ministry of Health, Ministry of Agriculture and Agro-based Industries [Department of Veterinary Services (DVS), Department of Fisheries (DOF), Department of Agriculture (DoA)], Department of Environment, Ministry of Higher Education, Ministry of Defence Hospitals, Private Healthcare Facilities, Community Pharmacist, The Animal Food Industry and Professional Organisations pertaining to Human And Animal Health) to address and mitigate AMR in respective sectors.This paper presents the aquaculture component of Malaysia' s NAP on AMR lead by the DOF, Malaysia.The objective of this paper is to briefly present the outcomes of activities carried out by the DOF in relation to AMR and AMU in Malaysia which includes: i) the development of the aquaculture component of the NAP; ii) results of the AMU survey; iii) outcome of AMR surveillance; iv) AMR education and awareness; and iv) strengthening governance.The initial AMR results indicate that most of the Escherichia coliisolates were resistant towards erythromycin (90.7 %), cefepime (26.6 %), tetracycline (18.2 %), ampicillin (15 %), and chloramphenicol (10 %).On the other hand, the majority of the Vibrio parahaemolyticus isolates were resistant to ampicillin (72.3 %) followed by erythromycin (10 %), cefotaxime (4 %), and tetracycline (4 %).
Barracuda fish (Sphyraena sp.) bone and fins could be a source of aquatic collagen. Marine collagen has recently gained popularity due to its lack of infectious infections. This collagen extraction yields 1.99 % acetic acid-soluble collagen (AAC), 2.36 % lactic acid-soluble collagen (LAC), and 3.26 % citric acid-soluble collagen (CAC). AAC has a high L* value compared to LAC and CAC, indicating great brightness in color. For hydroxyproline content, the amount of collagen was 82.70, 81.31, and 80.93 for AAC, LAC, and CAC. AAC and LAC have maximum collagen solubility at pH 3, and CAC at pH 5. The effects of collagen solubility on NaCl concentrations drop substantially at 30 g/L for all collagen samples. All extracted collagen structures are type I collagen consisting of two chains (α1 and α2) based on SDS-PAGE analysis and possessing a complete triple helical structure based on UV absorption (229.5 nm) and Fourier Transformation Infrared Spectrometry (ATR-FTIR) showed all collagen samples had amide A, B, amide I, II, and III peaks. All collagens demonstrate strong heat resistance and structural stability as Tmax is above 30°C. LAC demonstrated higher absorption of water (0.50 0.01±mL/mg) and oil (0.70±0.07 mL/mg) than AAC and CAC. At pH 7, CAC and AAC reduced foam and foam case capacity. In emulsion properties, only AAC does not demonstrate important emulsion stability. AAC showed superior collagen than LAC and CAC based on physicochemical and functional qualities. Therefore, all collagen samples can be employed as replacements for terrestrial collagen in diverse applications.
Fish collagens have gained considerable attention from numerous researchers due to their attractive traits and are more acceptable from most religious beliefs. This paper aimed to extract and characterize collagens from the skins of unicorn fish (N. reticulatus) influenced by pepsin from porcine (UCP) and pepsin from bovine (UCB). The yield of the UCP sample (15.60%) was significantly higher (P<0.05) compared to the UCB (10.40%). In addition to this, the swelling value of two collagens showed significant differences (P<0.05), with a greater percentage obtained in UCP 9261.23%) rather than UCB (196.75%). Both UCP and UCB were classified as type I collagen owing to the existence of two alpha chains under SDS-polyacrylamide gel electrophoresis. Under infrared and ultraviolet-visible parameters, the triple helical structure of collagens prepared using pepsin from porcine and bovine was preserved, and it was comparable to previous findings in fish collagen literature. All samples showed a different thermostability value, the higher one observed in the UCP (43.63°C) compared to the UCB sample (35.25°C), and their variations of thermostability were in agreement with the hydroxyproline content of UCP (83.57 mg/g) and UCB (81.47 mg/g). The unicorn fish (N. reticulatus) skin may be used as a good source of collagen, mainly utilized for industrial perspective.
More than 60% of the world surimi production is derived from tropical fish species and the percentage is increasing due to the rise in demand. Owing to the massive production, the by-products generated from surimi processing could pose a detrimental effect on the terrestrial and aquatic environment. To address this problem, traditionally efforts were made to convert these by-products into animal feeds, silages, fertilisers, and biofuels, which is in most cases, are considered as low value-added products. Since, fish surimi by-products possess valuable and predominant protein contents; hence, effective approaches are needed to exploit the by-products into high-end products such as collagen, gelatine, protein hydrolysate, peptide, enzymes that could be used in functional food, nutraceutical and pharmaceutical industries. This review focuses on the nutritional composition, value-added processing and biological active properties of by-products from tropical marine fish species processing. In addition, the use of these by-products as high-end products are also highlighted. This paper also discussed on the challenges on the utilisation of tropical fish by-products into high-value products. Utilisation of fish by-products into valuable food commodities would contribute on functional foods development and also on sustainable fish processing industry.
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