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The Inhibitory Properties of the Single-Chain 2S Albumin Seed Storage Protein from Theobroma cacao Karim, Norzulaiha Abd.; Budiman, Cahyo; Awang, Azwan; Rodrigues, Kenneth F.
Akta Agrosia Vol 28 No 1 (2025)
Publisher : Badan Penerbitan Fakultas Pertanian (BPFP), Fakultas Pertanian, Universitas Bengkkulu

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.31186/aa.28.1.8-14

Abstract

2S albumin seed storage proteins from Theobroma cacao (Tc-2S) are known for their roles in plant defense mechanisms due to their antimicrobial properties. However, it remains unclear whether both the light and heavy chains of Tc-2S are required for this activity. This study develops an expression system for the single-chain precursor of Tc-2S and evaluate its antimicrobial activity. Specifically, the heavy-chain subunit (Tc-9M), corresponding to residues 78 to 150 of the Tc-2S precursor, was cloned and expressed in a heterologous system. The resulting Tc-9M protein, expressed as a fully soluble protein, was purified via column chromatography, yielding 24 mg of pure protein from 300 mL of the expression culture. Antibacterial and antifungal activity was assessed using the Kirby-Bauer disc diffusion method, revealing that Tc-9M remarkably inhibited the growth of several bacterial strains, including Salmonella sp., Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Bacillus cereus. Additionally, Tc-9M inhibited the growth of the yeasts Saccharomyces cerevisiae and Pichia pastoris but showed no activity against the fungus Trichoderma asperellum. These findings ndicate that the single-chain Tc-2S may be sufficient for antimicrobial defense in plants. Because the characterization of the Tc-9M protein has not been previously reported, this work provides a basis for further exploration of the biological significance of the 2S albumin subunit in plant defense.  เว็บสล็อต Keywords: 2S albumin protein, antibacterial, antifungal, heavy-chain peptide, Theobroma cacao  
Physical, Chemical and Organoleptic Characteristics of Lactose-Free Milk-Based Ice Cream Arifin, Muhamad; Detiara, Azzahra; Arief, Irma Isnafia; Soenarno, Moch. Sriduresta; Fajr, Aulia Irhamni; Wulandari, Zakiah; Suryati, Tuti; Apriantini, Astari; ., Salundik; Murtini, Devi; Budiman, Cahyo; Taufik, Epi
Jurnal Teknologi Hasil Peternakan Vol 6, No 1 (2025): Maret
Publisher : Unpad Press

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24198/jthp.v6i1.61822

Abstract

Lactose-intolerant individuals avoid consuming milk and dairy products, which may lead to deficiencies in essential nutrients naturally present in milk. Lactose-free milk, characterized by its higher sweetness compared to full-cream milk, serves as an ideal base for ice cream—a widely consumed product valued for its sweetness and unique texture. This study aims to analyze the physical, chemical and organoleptic characteristics of lactose-free ice cream. Lactose-free milk was produced using 0.2% lactase enzyme. The evaluated parameters included viscosity, overrun, melting time, pH, sweetness level, total caloric content, lactose content, and organoleptic properties. Data were analyzed using a t-test by comparing ice cream made with whole milk and lactose-free milk. The results indicated that lactose-free ice cream exhibited a significantly higher overrun (p < 0.05), a sweeter taste, and lower total caloric content. However, it had a shorter melting time. No significant differences (p > 0.05) were observed in viscosity, pH, or organoleptic properties. These findings suggest that lactose-free ice cream demonstrates a comparable level of consumer acceptance to whole milk-based ice cream. Keywords: ice cream, lactase, lactose free milk, lactose intolerant,  whole milk
The Potential of Bioactive Peptides from Trypsin-Hydrolyzed Egg White of IPB-D1 Chicken as Antioxidant and Antibacterial Aryanti, Nova; Wulandari, Zakiah; Budiman, Cahyo
Jurnal Ilmu Pertanian Indonesia Vol. 30 No. 4 (2025): Jurnal Ilmu Pertanian Indonesia
Publisher : Institut Pertanian Bogor

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.18343/jipi.30.4.696

Abstract

The IPB-D1 chicken is the outcome of crossbreeding native Indonesian chickens and can produce eggs high in protein, which is excellent for bioactive peptide manufacturing. Egg white hydrolysates contain bioactive peptides with antioxidant and antibacterial properties. The purpose of this work was to assess the antioxidant and antibacterial properties of bioactive peptides produced from IPB-D1 egg white hydrolyzed with trypsin. The research procedures included determining the Haugh unit (HU) value, protein content, degree of hydrolysis (DH), and antioxidant and antibacterial activity. The hydrolysate inhibited DPPH by 44.82% and had an antioxidant capacity of 23.16 mg EVC 100/g. The hydrolysate had greater inhibition zones against Gram-positive and Gram-negative bacteria than the non-hydrolyzed egg white, indicating its antibacterial action. Inhibition zone sizes ranged from 2.42 to 3.48 mm. The findings show that enzymatic hydrolysis of IPB-D1 egg white with trypsin significantly improves its antioxidant and antibacterial properties. Keywords: antibacterial, antioxidant, bioactive peptide, IPB-D1 chicken, trypsin enzyme