Kholis Amalia Nofianti, Nia Safitri, Khomsya Ninteen Januar, Diajeng Putri Paramita, Norhayati, Luqmanul Hakim

Collagen and Gelatin Extraction from Manyung Bone Waste as Alternative Halal Raw Materials for Food Production

Introduction

Collagen and gelatin extraction from manyung bone waste as alternative halal raw materials for food production. Discover optimized methods for extracting halal collagen and gelatin from Manyung fish bone waste. This study offers a promising, cost-effective alternative for food and pharmaceutical applications.

Abstract

Collagen and gelatin are widely used in the food and pharmaceutical industries, yet their halal status remains a persistent concern for many products on the market. This study aimed to optimize the extraction and isolation of halal collagen and gelatin from Manyung fish bone waste, an abundant and low-cost Indonesian resource. Collagen was extracted at varying acid concentrations and reaction times, while gelatin was produced under eight treatment conditions varying in acid type, processing temperature, and extraction duration. Collagen and gelatin were characterized by Fourier Transform Infrared Spectroscopy (FTIR). In addition, the resulting gelatin was qualitatively examined using potassium dichromate and trinitrophenol solutions, which are commonly applied in Indonesia’s pharmaceutical industry. The FTIR spectrum of collagen showed absorption peaks corresponding to amide A, amide I, and amide II, whereas amide B and amide III bands were not detected. The highest collagen yield (4.4%) was obtained using 0.75 M acetic acid with a 5-day reaction time. For gelatin, FTIR confirmed the presence of characteristic amide A, amide B, amide I, amide II, and amide III bands. The optimal gelatin extraction was achieved with treatment 8, which involved immersion in 4% HCl, followed by 4% H₃PO₄, and extraction at 80°C for 6 hours, yielding 3.74%. Overall, these findings demonstrate that Manyung fish bone waste is a promising alternative source of halal collagen and gelatin, with potential applications in both food and pharmaceutical manufacturing.

Review

This study presents a timely and relevant investigation into the extraction and characterization of collagen and gelatin from Manyung fish bone waste, addressing the critical need for halal-certified raw materials in the food and pharmaceutical industries. The authors systematically optimized extraction parameters for both biopolymers, utilizing an abundant and cost-effective waste resource prevalent in Indonesia. The work successfully demonstrates the feasibility of isolating collagen and gelatin, with promising yields of 4.4% for collagen and 3.74% for gelatin under optimized conditions. The findings position Manyung fish bone waste as a viable and sustainable alternative source, offering a solution to current market concerns regarding the ethical and religious suitability of these widely used ingredients. The methodology employed in this research is commendable for its structured approach to process optimization. The authors explored a range of acid concentrations and reaction times for collagen, and a diverse set of acid types, temperatures, and durations for gelatin, ensuring a thorough search for optimal conditions. The use of Fourier Transform Infrared Spectroscopy (FTIR) provides essential structural conformation, confirming the presence of characteristic amide bands for both collagen and gelatin. Furthermore, the inclusion of qualitative tests using potassium dichromate and trinitrophenol, specifically highlighting relevance to the Indonesian pharmaceutical industry, demonstrates a practical focus and an awareness of local industrial needs. The successful identification of specific optimal parameters for extraction is a significant contribution to the field of sustainable biopolymer production. While the study offers valuable insights, the abstract points to areas that could enhance the comprehensiveness of the research. The observation that amide B and amide III bands were not detected in the collagen FTIR spectrum warrants further discussion, as these are typically characteristic of collagen and provide insights into its integrity. Although qualitative tests for gelatin are mentioned, their results are not presented in the abstract, leaving an information gap. For potential food and pharmaceutical applications, a more extensive characterization beyond FTIR would be beneficial, including analyses such as molecular weight distribution (e.g., SDS-PAGE), amino acid profiling, thermal stability, rheological properties, and safety assessments (e.g., heavy metal content). Future research could also focus on upscaling these optimized processes and conducting detailed comparative analyses with existing commercial halal collagen and gelatin products to validate their suitability for diverse industrial applications.

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