Highest Polygalacturonase Activity Research Articles

Valorization of black carrot pomace and pea powder for co-production of polygalacturonase and pectin lyase

AbstractPectic enzyme groups, particularly polygalacturonase and pectin lyase, are vital components of a high-value microbial enzyme category widely employed in applications within the fruit juice and wine industries. The exploration of alternative carbon and nitrogen sources remains crucial for enhancing enzyme production while reducing costs. This study evaluates the impact of carbon (black carrot pomace) and nitrogen (pea protein) loading on fermentable sugar content, protein content, and enzyme activities during both batch and fed-batch cultivation. Additionally, three distinct valorization techniques—thermal (steam), thermochemical (steam assisted with dilute acid), and microwave-assisted with dilute acid pretreatments—were assessed for their effectiveness in hydrolyzing black carrot pomace as a carbon source. The findings indicate that microwave-assisted dilute acid, coupled with enzymatic saccharification, resulted in the highest fermentable sugar production (0.493 g/g), achieving an 87.3% conversion yield. Pea protein demonstrated more favorable outcomes with the highest polygalacturonase activity (20.50 ± 0.52 U/L) and pectin lyase activity (46.44 ± 3.45 U/L) compared to whey protein and yeast extract used as nitrogen sources. Meanwhile, the highest polygalacturonase and pectin lyase activity, along with the highest total protein content (52.25 ± 0.06 mg/L), was recorded under the same culture conditions, reaching 164.34 ± 2.26 and 188.22 ± 1.72 U/L, respectively, after 72 h, representing approximately 1.18- and 1.34-fold increases from the batch system. Consequently, these results prove that fed-batch cultivation, utilizing black carrot pomace hydrolyzate as a feeding substrate and pea protein as a nitrogen source, significantly increases polygalacturonase and pectin lyase activity compared to batch cultivation.

Saccharogenic refining of Ginkgo biloba leaf residues using a cost-effective enzyme cocktail prepared by the fungal strain A32 isolated from ancient ginkgo biloba tree

To reduce environmental pollution and waste of biomass from Ginkgo biloba leaf residues (GBLRs), we developed a cost-effective enzyme system to hydrolyze GBLRs into available reducing sugars (RS). Biomass characteristics of GBLRs were investigated, which indicated that the acid hydrolyzed fraction was 49.43% of the dry weight of GBLRs. The fraction could be effectively converted into RS by an enzyme cocktail with high polygalacturonase activity without traditionally intricate pretreatment. The strain A32 isolated from the ancient ginkgo soil was used for the production of the enzyme cocktail, and a response surface methodology was used to optimize the enzymatic production. The enzyme cocktail released 87.2% of RS from GBLRs at 35 ℃ for 72 h with 1% (m/v) of loading, and the RS concentration arrived 8.95 ± 0.39 mg/ml with 9% of GBLRs loading. The cost-effective system of self-prepared enzyme cocktail is promising for facilitating GBLRs' bio-based industry.

Comparative evaluation of Aspergillus niger strains for endogenous pectin-depolymerization capacity and suitability for d-galacturonic acid production

Pectinaceous agricultural residues rich in d-galacturonic acid (d-GalA), such as sugar beet pulp, are considered as promising feedstocks for waste-to-value conversions. Aspergillus niger is known for its strong pectinolytic activity. However, while specialized strains for production of citric acid or proteins are well characterized, this is not the case for the production of pectinases. We, therefore, systematically compared the pectinolytic capabilities of six A. niger strains (ATCC 1015, ATCC 11414, NRRL 3122, CBS 513.88, NRRL 3, and N402) using controlled batch cultivations in stirred-tank bioreactors. A. niger ATCC 11414 showed the highest polygalacturonase activity, specific protein secretion, and a suitable morphology. Furthermore, d-GalA release from sugar beet pulp was 75% higher compared to the standard lab strain A. niger N402. Our study, therefore, presents a robust initial strain selection to guide future process improvement of d-GalA production from agricultural residues and identifies a high-performance base strain for further genetic optimizations.

Changes in morphogenesis and carotenogenesis to influence polygalacturonase secretion in Aspergillus carbonarius mutant.

Mycelial morphogenesis and the production of fungal secretory proteins are still largely unknown. A mutant strain of Aspergillus carbonarius UV-10046 produced abundant polygalacturonase (PG) along with partially saturated canthaxanthin (PSC) at low pH conditions. In the present study, the relationship between PG secretion and PSC biosynthesis was studied using carotenogenic inhibitors and SDS-PAGE electrophoresis. Also the correlation between morphogenesis and PG secretion was investigated by analysing through microscopic studies. From the results, it was observed that secretion of PG was positively influenced by the PSC biosynthesis. The results also showed that the mutant with hairy mycelial structure resulted in higher PG activity when compared to the wild type that lacks hyper branching. From the results, it was confirmed that a mutation might have occurred in the isoprenoid pathway that has helped mutant for survival at acidic conditions. Further, an alteration in the morphogenesis and hyper branching development caused over secretion of PG enzyme in the mutant.

Isolation of Polygalacturonase-Producing Bacterial Strain from Tomatoes (Lycopersicon esculentum Mill.).

Background Polygalacturonase (EC 3.2.1.15) enzyme aids in microbial spoilage of fruits and vegetables. It is very important to find economical ways to producing the enzyme so as to achieve maximum yield in industries due to its use at different areas of production process. Methods Isolation of polygalacturonase-producing bacterial strain from tomatoes (Lycopersicon esculentum Mill.) was studied. Polygalacturonase-producing bacterial strains were isolated and screened from tomatoes stored at normal laboratory temperature (25 ± 2°C). They were identified based on their morphological, biochemical, and molecular characteristics. The enzyme produced was partially purified by the ammonium sulphate precipitation method. Molecular weights and optimum conditions for best enzyme activity were obtained by SDS PAGE technique. Results Five bacterial isolates resulted after screening. Bacterial strain code B5 showed highest polygalacturonase activity. Optimum conditions for polygalacturonase PEC B5 were maintained at pH 4.5; temperature 35°C; substrate concentration 0.3 mg/ml, and best activity at less than 5 min of heating. The enzyme PEC B5 was found to weigh 65 kDa and 50 kDa for crude and partially purified aliquots, respectively. The result of 16S rRNA gene sequencing revealed bacterial strain code B5 as Enterobacter tabaci NR146667 having 79% similarity with the NCBI GenBank. Conclusion Microorganisms should be developed for large-scale production of enzymes in developing countries.

Toward Enhancing the Enzymatic Activity of a Novel Fungal Polygalacturonase for Food Industry: Optimization and Biochemical Analysis.

The review of literature and patents shows that enhancing the polygalacturonase (PG) production and activity are still required to fulfill the increasing demands. A dual optimization process, which involved Plackett-Burman design (PBD), with seven factors, and response surface methodology, was applied to optimize the production of extracellular PG enzyme produced by a novel strain of Aspergillus flavus isolated from rotten orange fruit. The fungal PG was purified and biochemically characterized. Three variables (harvesting time, pH and orange pomace concentration), that were verified to be significant by the PBD analysis, were comprehensively optimized via Box-Behnken design. According to this optimization, the highest PG activity (4073 U/mL) was obtained under pH 7 after 48 h using 40 g/L orange pomace as a substrate, with enhancement in PG activity by 51% compared to the first PBD optimization step. The specific activity of the purified PG was 1608 U/mg with polygalacturonic acid and its molecular weight was 55 kDa. The optimum pH was 5 with relative thermal stability (80%) at 50˚C after 30 min. The PG activity improved in the presence of Cu2+ and Ca2+, while Ba2+, Fe2+ and Zn2+ greatly inhibited the enzyme activity. The obvious Km and Vmax values were 0.8 mg/mL and 2000 μmol/min, respectively. This study is a starting point for initial research in the field of optimization and characterization of A. flavus PG. The statistical optimization of A. flavus PG and its biochemical characterization clearly revealed that this fungal strain can be a potential producer of PG which has a wide range of industrial applications.

Optimization of Pectinase Production by Aspergillus Oryzae RR 103

The purpose of this investigation is to isolate and Exploit diversified microorganisms from mangrove habitat and their commercial utilization in industrial sector. Pectinases are enzymes having a broad Industrial and commercial applications. Polygalacturonase produced by microorganisms which breakdown pectin, present in plant material to simple chemical substances. The enzymatic breakdown of α-1, 4-glycosidic linkages in polygalacturonic acid is catalysed by Polygalacturonic acid, releasing D-galacturonate which is a simple chemical substance. The production of Polygalacturonase by Aspergillus oryzae RR103 was enhanced by optimization of different nutritional parameters. Highest polygalacturonase activity was observed at 192h at 35°C. Optimum pH for the production of enhanced Polygalacturonic acid was at pH 6.0. The carbon and nitrogen sources which gave enhanced enzyme activity were Cellulose and Malt extract respectively. Highest enzyme specificity was recorded when the substrate used was citrus pectin. Polygalacturonase from Aspergillus oryzae RR 103 is suitable for industrial scale production as it has high productivity.

Screening and Characterization of Polygalacturonase as Potential Enzyme for Keprok Garut Orange (Citrus nobilis var. chrysocarpa) Juice Clarification

Use of thermostable enzyme from bacilli for industrial application is significant. This research aimed to isolate thermophilic pectinolytic bacteria from orange peel and vegetable waste which produced thermostable polygalacturonase, to investigate the polygalacturonase ability in clarifying keprok Garut orange juice, and to characterize polygalacturonase based on pH optimum, temperature optimum, enzyme stability, enzyme kinetics KM, and Vmax. Obtained, 14 isolates that further selected to 4 best isolates based on highest polygalacturonase activity and keprok Garut orange juice clarification ability. Four selected enzyme isolates were AR 2, AR 4, KK 4, and KK 5 had ability to increase juice transmittance, decrease juice viscosity and also reduce total soluble solid. Furthermore 4 selected isolates were partially purified by ammonium sulphate precipitation and dialysis method. Four partially purified enzymes were known that enzyme character of AR 2 optimum at pH 6; AR 4 optimum at pH 5.5; KK 4 optimum at pH 6; and KK 5 optimum at pH 4.5. Four enzymes were optimum at temperature 60°C thus stable at temperature 50-60°C, this characteristic indicate that enzymes were thermostable. AR 2 showed active activity stable at pH 4-7; AR 4 showed active activity stable at pH 6-7; KK 4 showed active activity stable at pH 4-6; however KK 5 stable at pH 4-5. Enzyme AR 2 and KK 4 was getting inactive at pH 11, thus AR 4 and KK 5 inactive at pH 12. KM value of AR 2, AR 4, KK 4, and KK 5 was 0.0959; 0.0974; 0.0966; and 0.178 mg/ml respectively. Vmax of AR 2, AR 4, KK 4, and KK 5 was 0.0203; 0.0202; 0.0185; and 0.0229 U/ml respectively. Enzyme AR 2 was the most compatible enzyme to be applied in keprok Garut orange juice clarification for it had the lowest KM value.

НОВЫЙ ОТЕЧЕСТВЕННЫЙ ФЕРМЕНТНЫЙ ПРЕПАРАТ ДЛЯ ВИНОДЕЛИЯ

A study into the effect of a new enzyme preparation Pectinol F-RKM 0719, used in the production of red table wines dur-ing maceration, was carried out. The investigated enzyme prepa-ration Pectinol F-RKM 0719 was previously isolated from the cul-ture liquid of the Aspergillus awamori F-RKM 0719 strain, ob-tained through multistage selection and mutagenesis at the De-partment of Biotechnology of the South Kazakhstan State Univer-sity named after M. Auezov. As a result of the development of a combined method of purification and isolation of a pectolytic en-zyme preparation, a preparation with a higher polygalacturonase activity was obtained having a sufficiently high yield of the desired product. The method is based on the sequential removal of individual groups of inactive impurities from the enzyme solutions using activated carbon and anion exchange resin. The use of hy-droxyapatite allows the activation of pectinases to be achieved by removing low molecular proteins. The absence of pectin substanc-es and carbohydrates makes it possible to use it in winemaking to clarify the best varieties of wine and remove the wine stone, which consists of the pectic substances of grape juice. The use of a new enzyme preparation in the process of maceration contributes to increasing the yield of mash from grape pulp, facilitating the pulp pressing and clarification of wine materials by reducing the vis-cosities and suspensions of the mash, as well as increasing the ex-traction of phenolic and colouring substances. The efficiency of enzymatic catalysis in the production of red table wines is demon-strated.

Polygalacturonase production by AR2 pectinolytic bacteria through submerged fermentation of raja nangka banana peel (Musa paradisiaca var. formatypica) with variation of carbon source and pectin

Polygalacturonase (EC 3.1.2.15) catalyzes the hydrolysis of α-1,4-glycosidic bonds on galacturonic acid. Polygalacturonase can be produced from AR2 pectinolytic bacteria isolated from orange peel and vegetable waste. Commonly cost production of enzymes were high. However, with the advancement of technology, enzymes can now be manufactured at a low cost. Production of enzymes in low cost media with agro-industrial waste is interesting. Raja nangka banana peel is agro-industrial waste that is uneconomic. Therefore, this material can be used as a pectin source in polygalacturonase production. Polygalacturonase was produced by AR2 pectinolytic bacteria with the addition of various carbon sources (1% glucose, 1% galactose, 1% lactose) and variation of pectin concentrations (5%; 7.5%; 10%). This study used submerged fermentation with a cultivation temperature of 55°C and an agitation speed of 144 rpm for a 48-h incubation time. The results showed that variation of carbon sources and pectin concentrations affected the production of polygalacturonase. After 48 h fermentation, the results showed that the number of cells of samples ranged from 8.3 to 9.445 log cells/mL; the used pectin of samples ranged from 87.170-93.745%; and the polygalacturonase activity of samples ranged from 0.030 to 0.151 U/mL. The highest polygalacturonase activity was obtained by production of polygalacturonase on 1% glucose and 10% pectin medium.

Partial purification of a polygalacturonase from a new Aspergillus sojae mutant and its application in grape mash maceration

SummaryThe use of polygalacturonase (PG) preparations in winemaking promotes the release of phenolic compounds. A PG from a new source, Aspergillus sojae mutant, was semi‐purified and tested for grape mash maceration. Crude extract (CE), a commercial pectinase, and two high PG activity semi‐purified preparations, FI and FII, were applied for maceration at PG activity of 3.5 U g−1 of grape for 46 h. Enzyme‐assisted maceration significantly (P < 0.05) increased the total phenolic content from 255.8 to 916.3 ± 5.2, 5732.9 ± 9.9, 563.4 ± 6.7 and 620.6 ± 18.4 mg L−1 for CE, commercial pectinase, FI and FII, respectively. The content of individual phenolics such as gallic, protocatechuic, chlorogenic and p‐coumaric acids was improved. Principal component and hierarchical clustering analyses suggested that CE has a better performance upon the release of phenols. Semi‐purified preparations acted similar to commercial pectinase. These findings open an opportunity for the potential use of PG from the mutant strain as an alternative macerating enzyme.

Uso do resíduo de laranja lima e da casca de coco verde na produção de enzimas

Com uma economia baseada na produção agrícola, o Nordeste brasileiro apresenta grandes volumes de resíduos que, quando não adequadamente dispostos, geram problemas ambientais e de saúde, devido à atração de insetos e roedores e o mau cheiro oriundos do processo de degradação. Como alternativa para minorar tais problemas e agregar valor aos resíduos, com a formação de produtos de interesse comercial, surgem os processos biotecnológicos. A aplicação da fermentação semi-sólida (FSS) é uma destas alternativas, destacando-se por ser um processo simples e de baixo custo. Avaliou-se neste trabalho o uso de resíduos agroindustriais como substrato para a produção de enzimas hidrolíticas por fermentação semi-sólida a partir do fungo Aspergillus niger, conduzidas em frascos Erlenmeyers de 250 mL suplementados com meio mineral, de forma a se ter um conteúdo final de umidade em torno de 60%. A cinética de crescimento foi acompanhada através de medida das atividades enzimáticas, acidez, pH, açúcares redutores (AR) e açúcares redutores totais (ART). Os resultados obtidos mostraram boa eficiência na produção de poligalacturonase ao utilizar resíduos de casca de coco verde, bagaço de laranja lima e a mistura dos dois resíduos como substrato, sendo a maior atividade poligalacturonásica 52,48 U/g, 22, 52 U/g e 38,68 U/g, respectivamente, com fraca atividade de pectinase em ambos. Obtiveram-se baixos valores para as atividades de avicelase e carboximetilcelulase para todos os resíduos, o que indica a necessidade de um pré-tratamento alcalino para promover maior indução enzimática.

Microbial strain improvement for enhanced polygalacturonase production by Aspergillus sojae

Strain improvement is a powerful tool in commercial development of microbial fermentation processes. Strains of Aspergillus sojae which were previously identified as polygalacturonase producers were subjected to the cost-effective mutagenesis and selection method, the so-called random screening. Physical (ultraviolet irradiation at 254 nm) and chemical mutagens (N-methyl-N'-nitro-N-nitrosoguanidine) were used in the development and implementation of a classical mutation and selection strategy for the improved production of pectic acid-degrading enzymes. Three mutation cycles of both mutagenic treatments and also the combination of them were performed to generate mutants descending from A. sojae ATCC 20235 and mutants of A. sojae CBS 100928. Pectinolytic enzyme production of the mutants was compared to their wild types in submerged and solid-state fermentation. Comparing both strains, higher pectinase activity was obtained by A. sojae ATCC 20235 and mutants thereof. The highest polygalacturonase activity (1,087.2 ± 151.9 U/g) in solid-state culture was obtained by mutant M3, which was 1.7 times increased in comparison to the wild strain, A. sojae ATCC 20235. Additional, further mutation of mutant M3 for two more cycles of treatment by UV irradiation generated mutant DH56 with the highest polygalacturonase activity (98.8 ± 8.7 U/mL) in submerged culture. This corresponded to 2.4-fold enhanced polygalacturonase production in comparison to the wild strain. The results of this study indicated the development of a classical mutation and selection strategy as a promising tool to improve pectinolytic enzyme production by both fungal strains.

Biochemical and physiological study of the firmness of table grape berries

Firmness is an essential quality parameter of table grapes (Vitis vinifera) for consumers, with grape bunches that contains soft berries less preferred, resulting in a reduction in the market price. The softening of grape berries has been commonly associated with cell walls, especially the disassembly of pectic polysaccharides. However, the process of berry softening is not completely understood. To investigate the softening process of grape berries, we compared the Thompson Seedless variety, which suffers significant economic losses due to fruit softening, and NN107, a new variety with a significantly higher level of berry firmness. The composition of the cell wall during the berry development of these two grape varieties was compared. NN107 berries had a greater amount of calcium and uronic acids in the cell wall material than Thompson Seedless grapes, suggesting a special role for calcium bridge formation in NN107. Additionally, polyacrylamide carbohydrate electrophoresis (PACE) analysis suggested differences between these varieties in pectin structure. Thompson Seedless grapes showed increased pectolyase hydrolysable site dynamics in the cell wall material and higher polygalacturonase activity than NN107. Immunohistochemistry focusing on the pectin structure confirmed the roles of both calcium bridge formation and cell wall integrity as they relate to a firmer grape berry phenotype.

Carbon, nitrogen and pH regulate the production and activity of a polygalacturonase isozyme produced by Penicillium expansum

The influence of carbon, nitrogen and pH on polygalacturonase (PG) activity produced by Penicillium expansum were investigated. P. expansum mycelial growth was greatest on lyophilized lyophilised fruit tissue and the highest PG activity occurred in apple pectin medium. Nitrogen source influenced PG activity and was highest with ammonia while the greatest mycelial mass was supported by glutamate or glutamine. PG activity and mycelial mass peaked 5 five days after inoculation as polyuronide content decreased and the pH and ammonium levels increased in apple pectin medium. A single active PG isozyme with an isoelectric point of ∼7.6 was produced in apple pectin medium and a partial cDNA clone was obtained that was most homologous to the pggII gene from Penicillium. griseoroseum. The results from this study indicate that P. expansum can modulate the activity of PG in response to nutrient sources and ambient pH through signalling pathways that modulate nutrient acquisition, uptake and metabolism.

Use of enzymes to elucidate the factors contributing to bitterness in rye flavour

In spite of the health-beneficial character of whole grain rye its use may be limited because of bitter taste. The impact of non-volatile chemical compounds on the bitter taste of rye was analysed by the aid of enzymatic hydrolysis, releasing potentially flavour-active compounds from the rye matrix. Whole grain rye flour–water suspension was treated with hydrolytic enzymes, whereafter portions of the rye suspensions were baked into crackers, assessed for their sensory profile as well as solubilised hydrolysis products. Heat treatment reduced the perceived bitterness. The treatment with enzyme preparation with high protease activity increased the bitterness of rye and also wheat flour both as suspension and as crackers. Other enzymes tested (with high polygalacturonase, endo-glucanase, xylanase or amyloglucosidase activity) had no significant impact on the perceived bitterness. Thus, small molecular weight peptides were considered to be a significant contributor to the bitter note of rye.

Pectinase enzyme-complex production by Aspergillus spp. in solid-state fermentation: A comparative study

A comparative evaluation of three Aspergillus species according to their pectinase production in solid-state fermentation was performed. Solid-state fermentation offers several potential advantages for enzyme production by fungal strains. Utilization of agricultural by-products as low-cost substrates for microbial enzyme production resulted in an economical and promising process. The pectinolytic enzyme activities of two Aspergillus sojae strains were compared to a known producer, Aspergillus niger IMI 91881, and to A. sojae ATCC 20235, which was re-classified as Aspergillus oryzae. Evaluation of polymethylgalacturonase and polygalacturonase activity was performed as well as exo- vs. endo-enzyme activity in the crude pectinase enzyme-complex of the mentioned strains. Furthermore, a plate diffusion assay was applied to determine the presence and action of proteases in the crude extracts. A. sojae ATCC 20235 with highest polymethylgalacturonase activity and highest polygalacturonase activity both exo- and endo-enzyme activity, is a promising candidate for industrial pectinase production, a group of enzymes with high commercial value, in solid-state fermentation processes. Beside the enzymatic assays a protein profile of each strain is given by SDS-PAGE electrophoresis and in addition species-specific zymograms for pectinolytic enzymes were observed, revealing the differences in protein pattern of the A. sojae strains to the re-classified A. oryzae.

Pectinolytic yeast isolates for cold-active polygalacturonase production

Abstract Pectin rich cold stored spoiled fruits, vegetables and cold soils were screened and different pectinolytic isolates were obtained by enrichment culturing and ruthenium red plate assay. Among the primary isolates 10–15% were yeast isolates. Six isolates with higher zones of pectin hydrolysis were selected and tested for polygalacturonase (PGU) production at room temperature (25 °C) and at 5 °C. One isolate identified as Saccharomyces sp. with highest polygalacturonase activity at 5 °C was used for enzyme production using raw fruit pectins as substrates. The isolate was identified by preliminary cultural, morphological and sugar fermentation tests. PGU production was high in raw pectin substrates like orange peel (21 U/ml), apple peel (20 U/ml ), mango peel (19 U/ml), grape must (18 U/ml) and guava peel (15 U/ml). Selected Saccharomyces sp. was found to grow at room temperature and produce good polygalacturonase active at 5 °C. Cold-active PGU could have ample application in fruit juice clarification as these conditions are milder and also prevent spoilage. The present study concentrated on enzyme production using the cheaper raw pectin rich substrates. Industrial relevance The manuscript contains information on the cold active polygalacturonase produced by yeast at room temperature. It has industrial application for fruit juice clarification at cold (mild) conditions as it is a cold active enzyme. Also the enzyme is produced at room temperature by yeast considered as a GRAS organism. Therefore, it is a significant observation by the authors.

Fungal isolates from natural pectic substrates for polygalacturonase and multienzyme production

Pectin rich wastes and waste dump yard soils were screened and eighty pectinolytic fungal isolates were obtained by enrichment culturing and ruthenium red plate assay. Eight isolates with higher zones of pectin hydrolysis were selected and tested for polygalacturonase production. One isolate identified as Aspergillus awamori MTCC 9166 with highest polygalacturonase activity was tested for utilization of raw pectins for enzyme production. Polygalacturonase production was high in raw pectin sources like Orange peel (16.8 U/ml) Jack fruit rind (38 U/ml) Carrot peel (36U/ml) and Beet root peel (24U/ml). Selected Aspergillus awamori MTCC 9166 was found to be having good polygalacturonase, xylanase, cellulase and weak amylase and protease activities. This isolate with multi-enzyme production could have application for enzymes production and degradation of fruit and vegetable waste in the process of urban waste disposal.

The effects of 1-methylcyclopropene on chilling and cell wall metabolism in loquat fruit

SummaryLoquat (Eriobotrya japonica L.) fruit were pre-treated with 0 (control) or 50 nl l–1 1-methylcyclopropene (1-MCP) for 24 h at 20°C, then stored at 1°C for 35 d to investigate the relationship between chilling injury and cell wall metabolism. Chilling increased fruit firmness and browning, and decreased the extractable juice content, with fewer symptoms of chilling injury in treated fruit. 1-MCP inhibited the activities of phenylalanine ammonia-lyase, cinnamyl alcohol dehydrogenase, 4-coumarate:coenzyme-A ligase, peroxidase, polyphenol oxidase, and slowed lignification. Treated fruit had a higher polygalacturonase activity, higher contents of water-soluble pectins, and lower contents of water-insoluble pectins compared with values in control fruit. These results suggest that the reduction in chilling injury in loquat caused by 1-MCP was primarily due to inhibition of lignin accumulation, a higher PG:PME ratio, and enhanced solubilisation of pectin in the cell walls.