Extraction, partial purification and characterization of proteases from the red seaweed Gracilaria edulis with similar cleavage sites on κ-casein as calf rennet

Arbita, Ariestya Arlene; Paul, Nicholas A.; Cox, Julian; Zhao, Jian

doi:10.1016/j.foodchem.2020.127324

Cited by 16 publications

(6 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The molecular weight distribution of casein in curd was studied using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) (Arbita et al ., 2020) with slight modifications. The curd lyophilised powder was dissolved in a phosphate buffer (0.5 mol/L, pH 7.0) to a concentration of 5 mg/mL.…”

Section: Methodsmentioning

confidence: 99%

“…It involves the enzyme‐mediated high‐specificity cleavage of κ‐CN at the Phe 105–Met 106 peptide bond that renders the casein micelles unstable and eventually causes aggregation, which leads to milk coagulation (Lucey et al ., 2003). The global demand for cheese is increasing every year and the demand for rennet is increasing, but enzymes used in cheese making have various drawbacks, hence, there is a continual need to find new coagulants (Arbita et al ., 2020). Currently, types of rennet mainly include plant‐derived rennet, microbially derived rennet, genetically engineered rennet and animal‐derived rennet.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effect of pH on the coagulation properties of Tenebrio molitor coagulant

Song

Zhang

Wen

et al. 2022

Int J of Food Sci Tech

View full text Add to dashboard Cite

Because of the continuous increase in global cheese consumption, there is a continual need to find new coagulants for producing cheeses with different characteristics to suit various consumers. A new coagulant was extracted from Tenebrio molitor larvae. We then investigated the influence of pH on the coagulation properties of Tenebrio molitor coagulant. The results indicate that the rennet flocculation time and whey OD value of Tenebrio molitor coagulant increased with the increase in coagulation pH (P < 0.05). The water holding capacity, turbidity, particle size and storage modulus increased and then decreased (P < 0.05) and reached the maximum at pH 5.6. There was a decrease and then increase for casein glycopeptide in the hydrolysis solution (P < 0.05), and its content reached 0.64 mg/mL at pH 6.2; the minimum hydrolysis of Tenebrio molitor coagulant was found at pH 5.6. SDS-PAGE, secondary structure and confocal laser scanning microscope indicated that the curd structure was stable at pH 5.6, and the coagulation performance was better. Moreover, there were the smallest differences for the texture structure of Tenebrio molitor coagulant curd with commercial rennet curd at pH 5.6. Therefore, pH 5.6 is the optimum pH of Tenebrio molitor coagulant. The study provides a theoretical basis and reference for the development of a new edible insect coagulant and its application.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effect of pH on the coagulation properties of Tenebrio molitor coagulant

Song

Zhang

Wen

et al. 2022

Int J of Food Sci Tech

View full text Add to dashboard Cite

show abstract

“…Electrophoresis was carried out at 100 V and 4°C for 4 h. The gels were later placed in proteolytic buffer of pH 7.4 containing 4 mM concentrations of CaCl 2 , 10 mM dithiothreitol (DTT) and 20 mM tris‐base at 27 ± 2°C for 18–24 h. The gel was later stained by 0.25% staining solution of Coomassie brilliant blue (CBB) additionally containing 10% (v/v) acetic acid and 40% (v/v) methanol for 30 min and afterward destained with 10% (v/v) acetic acid and 30% (v/v) methanol, until the gel becomes clear and bands become visible (Zhang et al, 2020). Gels were analyzed by white light illuminator for obtaining images (Arbita et al, 2020).…”

Section: Methodsmentioning

confidence: 99%

Casein zymography‐based detection and one‐step purification for simultaneous quantification of calcium‐induced endogenous proteases in breast and thigh muscles from different chicken breeds

Khoja

Arsalan

Biswas

et al. 2022

Food Processing Preservation

View full text Add to dashboard Cite

Identification and separation of endogenous proteases are important to find out their role in changes of biochemical process in post‐mortem muscle. Diverse studies were conducted to find out the activity of these enzymes but only a very few studies were carried out on avian species. In this study, a simple casein zymography method was explained for detection of calpain‐1 and calpain‐2 with the standardization of extraction buffer and that were quantified biochemically after one‐step separation and purification on anion exchange chromatography. DEAE Sephacel matrix was used to purify calpain‐1, calpain‐2, and calpastatin. SDS‐PAGE analysis showed native and autolyzed forms of calpains. Biochemical test indicated concentrations of calpain‐1, calpain‐2, and calpastatin being higher in breast than thigh muscles across all four breeds of chicken. A simple, effective, and low‐cost extraction, purification, and separation technique was developed for accurate identification of calpain‐1and calpain‐2 on casein zymography method and quantification by biochemical test. Novelty Impact Statement Identification and isolation of endogenous proteases are necessary to determine their significance in the PM aging of chicken meat from various breeds. In this study, a straightforward casein zymography approach for in‐vitro detection of calpain‐1 and calpain‐2 activity is devised. This will aid in the optimization of PM aging duration for meat tenderization.

show abstract

“…No setor de fabricação dos mais variados tipos de queijos a proteases protagonizam alguns eventos do processo como a coagulação e a maturação do queijo. O objetivo da coagulação no processamento de queijos é a concentração do leite e a retenção de gorduras, frequentemente para esses processos é utilizado um composto denominado coalho, que tem como componentes as proteases, quimosina e pepsina (ARBITA et al, 2020).…”

Section: Laticíniosunclassified

Inovação, Gestão e Sustentabilidade na Agroindústria

da¹,

Arcelino²,

de³

et al. 2021

View full text Add to dashboard Cite

Em 2021, ainda em meio à crise social gerada pela pandemia causada pelo Coronavírus, que levou a população a manter um distanciamento social, o CIAGRO foi planejado, conduzido e vivenciado dentro do cenário crescente de temas que envolvem a agroindústria mundial. Com o tema norteador “Inovação Gestão e Sustentabilidade na Agroindústria” o CIAGRO 2021 contemplou o que há de mais moderno para a agroindústria na atualidade. O Congresso Internacional da Agroindústria – CIAGRO 2021 é um evento, concebido no âmbito das atividades desenvolvidas no Programa Internacional Despertando Vocações para as Ciências Agrárias (PDVAgro) e realizado pelo Instituto Internacional Despertando Vocações (IIDV) que tem compromisso com a democratização do conhecimento e com uma educação de qualidade. O e-book volume 1 do CIAGRO 2021, está dividido em 26 capítulos que enfatiza os diversos elos da agroindústria, evidenciando alternativas para o desenvolvimento de pesquisas, desafios e expectativas para a cadeia produtiva dos alimentos, dividindo experiências nas áreas de Inovação, Gestão e Planejamento Agroindustrial.

show abstract

Extraction, partial purification and characterization of proteases from the red seaweed Gracilaria edulis with similar cleavage sites on κ-casein as calf rennet

Cited by 16 publications

References 28 publications

Effect of pH on the coagulation properties of Tenebrio molitor coagulant

Effect of pH on the coagulation properties of Tenebrio molitor coagulant

Casein zymography‐based detection and one‐step purification for simultaneous quantification of calcium‐induced endogenous proteases in breast and thigh muscles from different chicken breeds

Inovação, Gestão e Sustentabilidade na Agroindústria

Contact Info

Product

Resources

About